Displaying publications 81 - 100 of 288 in total

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  1. Ahola T, Couderc T, Courderc T, Ng LF, Hallengärd D, Powers A, et al.
    Vector Borne Zoonotic Dis, 2015 Apr;15(4):250-7.
    PMID: 25897811 DOI: 10.1089/vbz.2014.1681
    Currently, there are no licensed vaccines or therapies available against chikungunya virus (CHIKV), and these were subjects discussed during a CHIKV meeting recently organized in Langkawi, Malaysia. In this review, we chart the approaches taken in both areas. Because of a sharp increase in new data in these fields, the present paper is complementary to previous reviews by Weaver et al. in 2012 and Kaur and Chu in 2013 . The most promising antivirals so far discovered are reviewed, with a special focus on the virus-encoded replication proteins as potential targets. Within the vaccines in development, our review emphasizes the various strategies in parallel development that are unique in the vaccine field against a single disease.
    Matched MeSH terms: Viral Proteins/immunology
  2. Franklin F, Chong CW, Chua LH, Anthony AA, Liew MWO, Aziah I, et al.
    Med Microbiol Immunol, 2020 Oct;209(5):593-601.
    PMID: 32246197 DOI: 10.1007/s00430-020-00667-1
    Typhoid fever is a disease caused by Salmonella Typhi that was implicated in millions of illnesses worldwide annually. Individuals that do not recover fully from typhoid fever can become asymptomatic carriers of the disease. Host antibodies against the S. Typhi antigens, HlyE (for acute typhoid) and YncE (for carriers) were previously reported to be useful biomarkers for the disease. Here, we expressed and purified recombinant HlyE and YncE antigens and tested the IgG, IgA and IgM responses in 422 sera samples retrieved from acute typhoid patients, other febrile, food handlers, and healthy individuals. The results showed that HlyE-IgG, -IgA and -IgM ELISAs have a collective sensitivity of 83% while YncE-IgG and -IgA ELISAs identified 16 possible carriers based on their antibody profiles. The identification of sensitive biomarkers for typhoid carrier detection is crucial for disease eradication.
    Matched MeSH terms: Hemolysin Proteins/immunology*
  3. Mohd Amiruddin MN, Ang GY, Yu CY, Falero-Diaz G, Otero O, Reyes F, et al.
    J Microbiol Methods, 2020 09;176:106003.
    PMID: 32702386 DOI: 10.1016/j.mimet.2020.106003
    Mycobacterium tuberculosis (Mtb) is a pathogenic bacterium that causes tuberculosis (TB). This contagious disease remains a severe health problem in the world. The disease is transmitted via inhalation of airborne droplets carrying Mtb from TB patients. Early detection of the disease is vital to prevent transmission of the infection to people in close contact with the patients. To date, there is a need of a simple, rapid, sensitive and specific diagnostic test for TB. Previous studies showed the potential of Mtb 16 kDa antigen (Ag16) in TB diagnosis. In this study, lateral flow immunoassay, also called simple strip immunoassay or immunochromatographic test (ICT) for detection of Ag16 was developed (Mtb-strip) and assessed as a potential rapid TB diagnosis method. A monoclonal antibody against Ag16 was optimized as the capturing and detection antibody on the Mtb-strip. Parameters affecting the performance of the Mtb-strip were also optimized before a complete prototype was developed. Analytical sensitivity showed that Mtb-strip was capable to detect as low as 125 ng of purified Ag16. The analytical sensitivity of Mtb-strip suggests its potential usefulness in different clinical applications.
    Matched MeSH terms: Bacterial Proteins/immunology*
  4. Tan NH, Lim KK, Jaafar MI
    Toxicon, 1993 Jul;31(7):865-72.
    PMID: 8212031
    The antigenic cross-reactivity of four Ophiophagus hannah (king cobra) venom components, the neurotoxin (OH-NTX), phospholipase A2 (OH-PLA2), hemorrhagin (OH-HMG) and L-amino acid oxidase (OH-LAAO) were examined by indirect and double sandwich ELISAs. The indirect ELISAs for OH-NTX, OH-PLA2 and OH-HMG were very specific when assayed against the various heterologous snake venoms and O. hannah venom components, at 25 ng/ml antigen level. At higher antigen concentrations (100-400 ng/ml), there were moderate to strong indirect ELISA cross-reactions between anti-O. hannah neurotoxin and venoms from various species of cobra as well as two short neurotoxins. However, anti-O. hannah hemorrhagin did not cross-react with any of the venoms tested, even at these high antigen concentrations, indicating that O. hannah hemorrhagin is antigenically very different from other venom hemorrhagins. Examination of the indirect ELISA cross-reactions between anti-O. hannah PLA2 and several elapid PLA2 enzymes suggests that the elapid PLA2 antigenic class has more than two subgroups. The antibodies to O. hannah L-amino acid oxidase, however, yielded indirect ELISA cross-reactions with many venoms as well as with OH-NTX, OH-PLA2 and OH-HMG, indicating that OH-LAAO shares common epitopes even with unrelated proteins. The double sandwich ELISAs for the four anti-O. hannah venom components, on the other hand, generally exhibited a higher degree of selectivity than the indirect ELISA procedure.
    Matched MeSH terms: Cobra Neurotoxin Proteins/immunology*
  5. Camalxaman SN, Zeenathul NA, Quah YW, Loh HS, Zuridah H, Sheikh-Omar AR, et al.
    Trop Biomed, 2011 Dec;28(3):661-7.
    PMID: 22433897 MyJurnal
    This study probes into the prospect of cross-reactivity of HCMV with RCMV which has not been acknowledged to date. We describe the uncovering of a protein with an estimated size of between 61-68 kDa from local RCMV strains which reacted with HCMV positive sera. Our findings are a first disclosure of a plausible immunological cross-reactivity between RCMV with its human counterpart which grounds substantial interest implying existence of conserved determinants between rat and human CMV polypeptides. The cross-reactive protein most likely represents an enveloped glycoprotein, though the precise identification and its degree of similarity needs to be evidently defined and further elucidated in forthcoming experiments.
    Matched MeSH terms: Viral Proteins/immunology*
  6. Rosmilah M, Shahnaz M, Masita A, Noormalin A, Jamaludin M
    Trop Biomed, 2005 Dec;22(2):171-7.
    PMID: 16883284 MyJurnal
    Fish has been recognized as a source of potent allergens both in food and occupational allergy. Lutjanus argentimaculatus (red snapper) and Lutjanus johnii (golden snapper) locally known as merah and jenahak, respectively, are among the most commonly consumed fish in Malaysia. The objective of this study is to identify the IgE-binding proteins and major allergens of these species of fishes. Extracts of both fish species were prepared and fractionated by sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE). IgE binding patterns were then demonstrated by immunoblotting using sera from patients allergic to the fishes. The raw extracts of both fish produced 26 protein bands. Both species of fishes had similar protein profiles. In cooked extracts, several protein bands in the range of about 40 to 90 kD which were present in the uncooked extracts appeared to be denatured and formed high molecular weight complexes. The immunoblotting of golden snapper and red snapper revealed 16 and 15 various IgE-binding bands, in the range of 151 to 12-11 kD, respectively. A 51 kD protein was identified as a major allergen for both fishes. A 46 kD protein was also demonstrated as a major allergen in golden snapper and a 42 kD protein was also seen as a major allergen in red snapper. A heat-resistant protein of ~12 kD which is equivalent in size with fish parvalbumin was demonstrated only as minor allergen for both fishes.
    Matched MeSH terms: Proteins/immunology
  7. Dielievska V, Korzh M, Leontieva F, Ashukina N, Borzova O
    Arch Razi Inst, 2020 06;75(2):257-265.
    PMID: 32621457 DOI: 10.22092/ari.2020.341761.1439
    This study investigated a person with an AB0 discrepancy. Her blood group initially typed at the birth as AB Rh+ (positive); however, it was B Rh+ (positive) or Rh- (negative) when she was in her teens. At room temperature, her erythrocytes were agglutinated by anti-B, and the agglutination was significantly weaker at 37 ºC. As a result, her erythrocytes did not absorb anti-B but anti-A. Furthermore, her erythrocytes were agglutinated by anti-A at 37 ºC with signs of hemolysis in the presence of complement. The unwashed erythrocytes were also agglutinated in an antiglobulin test by polyclonal anti-A at 37 ºC and by heated polyclonal anti-A and anti-A MAB 2-8 at room temperature. Moreover, her serum agglutinated A erythrocytes at room temperature with less activity at 37 ºC; however, it agglutinated B erythrocytes at 37 ºC. The ability of the erythrocytes of this person to absorb anti-A came along with the agglutination of her erythrocytes at 37 ºC by polyclonal serum and decreased activity of the serum to agglutinate A erythrocytes at 37 ºC, compared to room temperature. The absence of anti-B absorbance by the person’s erythrocytes was accompanied by the presence of anti-B in the serum, which was active at 37 ºC. The incubation of the person’s serum with 0 erythrocytes induced the ability of erythrocytes to absorb anti-A and to be hemolyzed by anti-A in the presence of complement in accordance with the person’s characteristics of erythrocytes. The reaction of absorption and agglutination at room temperature and 37 ºC by heated serum with the use of complement may help to reveal both weak A and B antigens and anti-A and anti-B antibodies while AB0 blood typing.
    Matched MeSH terms: Complement System Proteins/immunology
  8. Hashim OH, Gendeh GS, Cheong CN, Jaafar MI
    Immunol Invest, 1994 Mar;23(2):153-60.
    PMID: 8194855
    The effect of Artocarpus integer lectin (lectin C) on the functional activity of guinea-pig complement was investigated. Purified and crude extract of lectin C from six cultivars of Artocarpus integer seeds were found to consume complement and thus decreased the complement-induced haemolytic activity of sensitized sheep erythrocytes. The change in the complement-mediated haemolytic activity was significantly decreased when incubation of the lectins was performed in the presence of melibiose. The reversal effect of the carbohydrate, which is a potent inhibitor of the lectin's binding to O-linked oligosaccharides of glycoprotein, demonstrate involvement of the lectins interaction with O-glycans of glycoproteins in the consumption of guinea-pig complement.
    Matched MeSH terms: Complement System Proteins/immunology*
  9. Hasan NH, Ebrahimie E, Ignjatovic J, Tarigan S, Peaston A, Hemmatzadeh F
    PLoS One, 2016;11(6):e0156418.
    PMID: 27362795 DOI: 10.1371/journal.pone.0156418
    A common approach for developing diagnostic tests for influenza virus detection is the use of mouse or rabbit monoclonal and/or polyclonal antibodies against a target antigen of the virus. However, comparative mapping of the target antigen using antibodies from different animal sources has not been evaluated before. This is important because identification of antigenic determinants of the target antigen in different species plays a central role to ensure the efficiency of a diagnostic test, such as competitive ELISA or immunohistochemistry-based tests. Interest in the matrix 2 ectodomain (M2e) protein of avian influenza virus (AIV) as a candidate for a universal vaccine and also as a marker for detection of virus infection in vaccinated animals (DIVA) is the rationale for the selection of this protein for comparative mapping evaluation. This study aimed to map the epitopes of the M2e protein of avian influenza virus H5N1 using chicken, mouse and rabbit monoclonal or monospecific antibodies. Our findings revealed that rabbit antibodies (rAbs) recognized epitope 6EVETPTRN13 of the M2e, located at the N-terminal of the protein, while mouse (mAb) and chicken antibodies (cAbs) recognized epitope 10PTRNEWECK18, located at the centre region of the protein. The findings highlighted the difference between the M2e antigenic determinants recognized by different species that emphasized the importance of comparative mapping of antibody reactivity from different animals to the same antigen, especially in the case of multi-host infectious agents such as influenza. The findings are of importance for antigenic mapping, as well as diagnostic test and vaccine development.
    Matched MeSH terms: Viral Matrix Proteins/immunology*
  10. Miah G, Rafii MY, Ismail MR, Puteh AB, Rahim HA, Latif MA
    J Sci Food Agric, 2017 Jul;97(9):2810-2818.
    PMID: 27778337 DOI: 10.1002/jsfa.8109
    BACKGROUND: The rice cultivar MR219 is famous for its better yield and long and fine grain quality; however, it is susceptible to blast disease. The main objective of this study was to introgress blast resistance genes into MR219 through marker-assisted selection (MAS). The rice cultivar MR219 was used as the recurrent parent, and Pongsu Seribu 1 was used as the donor.

    RESULTS: Marker-assisted foreground selection was performed using RM6836 and RM8225 to identify plants possessing blast resistance genes. Seventy microsatellite markers were used to estimate recurrent parent genome (RPG) recovery. Our analysis led to the development of 13 improved blast resistant lines with Piz, Pi2 and Pi9 broad-spectrum blast resistance genes and an MR219 genetic background. The RPG recovery of the selected improved lines was up to 97.70% with an average value of 95.98%. Selected improved lines showed a resistance response against the most virulent blast pathogen pathotype, P7.2. The selected improved lines did not express any negative effect on agronomic traits in comparison with MR219.

    CONCLUSION: The research findings of this study will be a conducive approach for the application of different molecular techniques that may result in accelerating the development of new disease-resistant rice varieties, which in turn will match rising demand and food security worldwide. © 2016 Society of Chemical Industry.

    Matched MeSH terms: Plant Proteins/immunology
  11. Chin VK, Basir R, Nordin SA, Abdullah M, Sekawi Z
    Int Microbiol, 2020 May;23(2):127-136.
    PMID: 30875033 DOI: 10.1007/s10123-019-00067-3
    Human leptospirosis is considered as one of the most widespread and potentially fatal zoonotic diseases that causes high mortality and morbidity in the endemic regions of tropical and subtropical countries. The infection can arise from direct or indirect exposure of human through contaminated environment that contains leptospires or animal reservoirs that carry leptospires. The clinical manifestations during human leptospirosis ranges from asymptomatic, mild infections to severe and life-threatening complications involving multi-organ failures with kidneys, lungs and liver severely affected. Despite much efforts have been put in to unravel the pathogenesis during human leptospirosis, it remains obscure to which extent the host factors or the pathogen itself contribute towards the pathogenesis. Host innate immunity, especially, polymorphonuclear neutrophils and complement system are involved in the first line of defense during human leptospirosis. However, pathogenic Leptospira has acquired diverse evasion strategies to evade from host immunity and establish infection in infected hosts. Hence, in this review, we focus on organs pathology during human leptospiral infection and host evasion strategies employed by Leptospira. A profound understanding on leptospiral immunity and how Leptospira subvert the immune system may provide new insights on the development of therapeutic regimens against this species in future.
    Matched MeSH terms: Complement System Proteins/immunology
  12. Hu D, Zhu Z, Li S, Deng Y, Wu Y, Zhang N, et al.
    PLoS Pathog, 2019 06;15(6):e1007836.
    PMID: 31242272 DOI: 10.1371/journal.ppat.1007836
    Dengue is the most widespread vector-borne viral disease caused by dengue virus (DENV) for which there are no safe, effective drugs approved for clinical use. Here, by using sequential antigen panning of a yeast antibody library derived from healthy donors against the DENV envelop protein domain III (DIII) combined with depletion by an entry defective DIII mutant, we identified a cross-reactive human monoclonal antibody (mAb), m366.6, which bound with high affinity to DENV DIII from all four DENV serotypes. Immunogenetic analysis indicated that m366.6 is a germline-like mAb with very few somatic mutations from the closest VH and Vλ germline genes. Importantly, we demonstrated that it potently neutralized DENV both in vitro and in the mouse models of DENV infection without detectable antibody-dependent enhancement (ADE) effect. The epitope of m366.6 was mapped to the highly conserved regions on DIII, which may guide the design of effective dengue vaccine immunogens. Furthermore, as the first germline-like mAb derived from a naïve antibody library that could neutralize all four DENV serotypes, the m366.6 can be a tool for exploring mechanisms of DENV infection, and is a promising therapeutic candidate.
    Matched MeSH terms: Viral Envelope Proteins/immunology*
  13. Yunus MH, Arifin N, Balachandra D, Anuar NS, Noordin R
    Am J Trop Med Hyg, 2019 08;101(2):432-435.
    PMID: 31218996 DOI: 10.4269/ajtmh.19-0053
    The conventional method of detecting Strongyloides stercoralis in fecal samples has poor diagnostic sensitivity. Detection of Strongyloides-specific antibodies increases the sensitivity; however, most tests are ELISAs that use parasite extract which may cross-react with the sera of other helminth infections. To improve the serological diagnosis of strongyloidiasis, this study aimed at developing a sensitive and specific lateral flow rapid dipstick test. Two recombinant proteins, recombinant NIE (rNIE) and recombinant Ss1a (rSs1a), were used in preparing the dipstick, with gold-conjugated antihuman IgG4 as detector reagent. In parallel, the corresponding ELISA was performed. Both assays demonstrated diagnostic sensitivity of 91.3% (21/23) when tested with serum samples of patients with Strongyloides infection, and 100% specificity with 82 sera of asymptomatic (healthy) and those with other parasitic infections. The ELISA and dipstick test results were positively correlated to each other (r = 0.6114, P = 0.0019). The developed lateral flow dipstick test may improve the serodiagnosis of strongyloidiasis and merit further validation studies.
    Matched MeSH terms: Recombinant Proteins/immunology
  14. Vishalkumar P, Jayaprakash NS, Desai PK, Krishnan V, Vijayalakshmi MA
    Trop Biomed, 2020 Dec 01;37(4):1050-1061.
    PMID: 33612757 DOI: 10.47665/tb.37.4.1050
    OBJECTIVE: To evaluate the sensitivity and the stability of the monoclonal antibodies (Aa3c10, b10c1), against truncated Histidine-rich protein 2 (PfHRP2), developed using smart polymer, poly N-isopropylacrylamide, as adjuvant for malarial diagnostic applications in comparison with the available commercial antibodies.

    METHODS: Two hybridoma clones (Aa3c10, b10c1) were used for the production of ascites in BALB/c mice. Purification of monoclonal antibodies from the ascites was carried out using affinity columns. The thermal stability study of monoclonal antibodies was done by storing it at 37°C and 45°C for thirty days. The stored antibodies were analyzed using SDS-PAGE and flow-through device where the antigenantibody interaction was visualized by Protein A colloidal gold solution. Sensitivity was determined by endpoint dilution ELISA and the dissociation constant by competitive ELISA. Sensitive pair optimization was done by sandwich ELISA using biotinylated antibodies. Prototype preparation for lateral flow assay had a colloidal gold-based detection system.

    RESULTS: Thermal stability experiments showed that both mAbs (Aa3c10; b10c1) are stable up to thirty days at 45°C while the commercially available mAbs were stable up to fifteen days only. Compared to commercial antibodies, the mAb Aa3c10, showed the highest sensitivity in end-point titre. In sensitive pair optimization, it was observed that the mAb, b10c1, as a detector and the mAb, Aa3c10, as a capture antibody showed the highest absorbance to detect 50pg/ml PfHRP2 antigen. The prototype formulation of lateral flow assay using the mAbs (Aa3c10; b10c1) showed good reactivity with WHO panel and no false-positive results were observed with twenty clinically negative samples and five P. vivax positive samples.

    CONCLUSIONS: The novel monoclonal antibodies (Aa3c10, b10c1) against truncated PfHRP2, could be a strong potential candidates that can be included in making RDTs with better sensitivity and stability.

    Matched MeSH terms: Protozoan Proteins/immunology*
  15. Azemi NFH, Misnan R, Keong BP, Mokhtar M, Kamaruddin N, Fah WC, et al.
    Mol Biol Rep, 2021 Oct;48(10):6709-6718.
    PMID: 34427887 DOI: 10.1007/s11033-021-06661-x
    BACKGROUND: Tropomyosin is a major allergen in crustaceans, including mud crab species, but its molecular and allergenic properties in Scylla olivacea are not well known. Thus, this study aimed to produce the recombinant tropomyosin protein from S. olivacea and subsequently investigate its IgE reactivity.

    METHODS AND RESULTS: The tropomyosin gene was cloned and expressed in the Escherichia coli system, followed by SDS-PAGE and immunoblotting test to identify the allergenic potential of the recombinant protein. The 855-base pair of tropomyosin gene produced was found to be 99.18% homologous to Scylla serrata. Its 284 amino acids matched the tropomyosin of crustaceans, arachnids, insects, and Klebsiella pneumoniae, ranging from 79.03 to 95.77%. The tropomyosin contained 89.44% alpha-helix folding with a tertiary structure of two-chain alpha-helical coiled-coil structures comprising a homodimer heptad chain. IPTG-induced histidine tagged-recombinant tropomyosin was purified at the size of 42 kDa and confirmed as tropomyosin using anti-tropomyosin monoclonal antibodies. The IgE binding of recombinant tropomyosin protein was reactive in 90.9% (20/22) of the sera from crab-allergic patients.

    CONCLUSIONS: This study has successfully produced an allergenic recombinant tropomyosin from S. olivacea. This recombinant tropomyosin may be used as a specific allergen for the diagnosis of allergy.

    Matched MeSH terms: Recombinant Proteins/immunology*
  16. Leong SW, Lim TS, Ismail A, Choong YS
    J. Mol. Recognit., 2018 05;31(5):e2695.
    PMID: 29230887 DOI: 10.1002/jmr.2695
    With the development of de novo binders for protein targets from non-related scaffolds, many possibilities for therapeutics and diagnostics have been created. In this study, we described the use of de novo design approach to create single-chain fragment variable (scFv) for Salmonella enterica subspecies enterica serovar Typhi TolC protein. Typhoid fever is a global health concern in developing and underdeveloped countries. Rapid typhoid diagnostics will improve disease management and therapy. In this work, molecular dynamics simulation was first performed on a homology model of TolC protein in POPE membrane bilayer to obtain the central structure that was subsequently used as the target for scFv design. Potential hotspot residues capable of anchoring the binders to the target were identified by docking "disembodied" amino acid residues against TolC surface. Next, scFv scaffolds were selected from Protein Data Bank to harbor the computed hotspot residues. The hotspot residues were then incorporated into the scFv scaffold complementarity determining regions. The designs recapitulated binding energy, shape complementarity, and interface surface area of natural protein-antibody interfaces. This approach has yielded 5 designs with high binding affinity against TolC that may be beneficial for the future development of antigen-based detection agents for typhoid diagnostics.
    Matched MeSH terms: Bacterial Outer Membrane Proteins/immunology*
  17. Kumaran SK, Bakar MFA, Mohd-Padil H, Mat-Sharani S, Sakinah S, Poorani K, et al.
    Acta Trop, 2017 Dec;176:433-439.
    PMID: 28941729 DOI: 10.1016/j.actatropica.2017.09.011
    Leptospirosis is a widespread zoonotic disease caused by pathogenic Leptospira species (Leptospiraceae). LipL32 is an abundant lipoprotein from the outer membrane proteins (OMPs) group, highly conserved among pathogenic and intermediate Leptospira species. Several studies used LipL32 as a specific gene to identify the presence of leptospires. This research was aimed to study the characteristics of LipL32 protein gene code, to fill the knowledge gap concerning the most appropriate gene that can be used as antigen to detect the Leptospira. Here, we investigated the features of LipL32 in fourteen Leptospira pathogenic strains based on comparative analyses of their primary, secondary structures and 3D modeling using a bioinformatics approach. Furthermore, the physicochemical properties of LipL32 in different strains were studied, shedding light on the identity of signal peptides, as well as on the secondary and tertiary structure of the LipL32 protein, supported by 3D modelling assays. The results showed that the LipL32 gene was present in all the fourteen pathogenic Leptospira strains used in this study, with limited diversity in terms of sequence conservation, hydrophobic group, hydrophilic group and number of turns (random coil). Overall, these results add basic knowledge to the characteristics of LipL32 protein, contributing to the identification of potential antigen candidates in future research, in order to ensure prompt and reliable detection of pathogenic Leptospira species.
    Matched MeSH terms: Bacterial Outer Membrane Proteins/immunology
  18. NikNadia N, Tan CW, Ong KC, Sam IC, Chan YF
    J Med Virol, 2018 06;90(6):1164-1167.
    PMID: 29457642 DOI: 10.1002/jmv.25061
    Enterovirus A71 (EV-A71) neutralization escape mutants were generated with monoclonal antibody MAB979 (Millipore). The VP2-T141I and VP1-D14N substitutions were identified. Using reverse genetics, infectious clones with these substitutions were constructed and tested by neutralization assay with immune sera from mice and humans. The N-terminus VP1-14 is more important than EF loop VP2-141 in acute human infection, mainly because it recognised IgM present in acute infection. The N-terminus VP1 could be a useful target for diagnostics and therapeutic antibodies in acute infection.
    Matched MeSH terms: Capsid Proteins/immunology*
  19. Ng WK, Lim TS, Lai NS
    Biotechnol Appl Biochem, 2018 Jul;65(4):547-553.
    PMID: 29280199 DOI: 10.1002/bab.1636
    A critical challenge in producing an antibody-based assay with the highest reproducibility and sensitivity is the strategy to immobilize antibodies to solid phase. To date, numerous methods of antibody immobilization were reported but each was subjected to its advantages and limitations. The current study proposes a new potential antibody binding protein, the human neonatal fragment crystallizable (Fc) receptor. This protein has shown its high affinity to the Fc of antibody either in vivo or in vitro. Human neonatal Fc receptor is a heterodimer constructed by p51 α-heavy chain and β2-microglobulin light chain; however, the binding sites toward the antibody are located in the p51 α-heavy chain. Hence, vector cloning and recombinant protein expression were carried out to express the p51 α-heavy chain of the human neonatal Fc receptor (hFcRn-α). The recombinant protein expressed, hFcRn-α, was adopted to pin rabbit IgG against hepatitis B virus surface antigen to a solid phase. A sandwich enzyme-linked immunosorbent assay was further developed to evaluate the efficiency of hFcRn-α-directed immobilization in antigen detection. The result was compared with the conventional physical adsorption method. The findings demonstrated that human neonatal Fc receptor was efficient in pinning antibodies and generating higher signals compared with the physical adsorption of antibody.
    Matched MeSH terms: Recombinant Proteins/immunology
  20. Chia KY, Ng KY, Koh RY, Chye SM
    CNS Neurol Disord Drug Targets, 2018;17(9):671-679.
    PMID: 29546836 DOI: 10.2174/1871527317666180315161626
    BACKGROUND & OBJECTIVE: Protein misfolding and aggregation have been considered the common pathological hallmarks for a number of neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease (HD). These abnormal proteins aggregates damage mitochondria and induce oxidative stress, resulting in neuronal cell death. Prolonged neuronal damage activates microglia and astrocytes, development of inflammation reaction and further promotes neurodegeneration. Thus, elimination of abnormal protein aggregates without eliciting any adverse effects are the main treatment strategies. To overcome this, recent studies have deployed single- chain fragment variable antibodies (scFvs) to target the pathological protein aggregates, such as amyloid-beta (Aβ) peptides, α-synuclein (α-syn) and Huntingtin (Htt). To date scFv has been effective at inhibiting abnormal protein aggregates formation in both in vitro and in vivo model system of AD, PD and HD.

    CONCLUSION: Currently active research is still ongoing to improve the scFv gene delivery technology, to further enhance brain penetration, intracellular stability, solubility and efficacy of scFv intrabody.

    Matched MeSH terms: Amyloidogenic Proteins/immunology
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