Displaying publications 81 - 100 of 528 in total

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  1. Cloning, expression and characterization of a novel cold‑adapted GDSL family esterase from Photobacterium sp. strain J15
    Shakiba MH, Ali MS, Rahman RN, Salleh AB, Leow TC
    Extremophiles, 2016 Jan;20(1):44-55.
    PMID: 26475626 DOI: 10.1007/s00792-015-0796-4
    The gene encoding for a novel cold-adapted enzyme from family II of bacterial classification (GDSL family) was cloned from the genomic DNA of Photobacterium sp. strain J15 in an Escherichia coli system, yielding a recombinant 36 kDa J15 GDSL esterase which was purified in two steps with a final yield and purification of 38.6 and 15.3 respectively. Characterization of the biochemical properties showed the J15 GDSL esterase had maximum activity at 20 °C and pH 8.0, was stable at 10 °C for 3 h and retained 50 % of its activity after a 6 h incubation at 10 °C. The enzyme was activated by Tween-20, -60 and Triton-X100 and inhibited by 1 mM Sodium dodecyl sulphate (SDS), while β-mercaptoethanol and Dithiothreitol (DTT) enhanced activity by 4.3 and 5.4 fold respectively. These results showed the J15 GDSL esterase was a novel cold-adapted enzyme from family II of lipolytic enzymes. A structural model constructed using autotransporter EstA from Pseudomonas aeruginosa as a template revealed the presence of a typical catalytic triad consisting of a serine, aspartate, and histidine which was verified with site directed mutagenesis on active serine.
    Matched MeSH terms: Amino Acid Sequence
  2. Fulltext Molecular cloning, sequence analysis and developmental stage expression of a putative septin gene fragment from Aedes albopictus (Diptera: Culicidae)
    Avicor SW, Wajidi MF, Jaal Z, Yahaya ZS
    Acta Biochim. Pol., 2016;63(2):243-6.
    PMID: 27059016 DOI: 10.18388/abp.2014_909
    Septins belong to GTPases that are involved in vital cellular activities, including cytokinesis. Although present in many organisms, they are yet to be isolated from Aedes albopictus. This study reports for the first time on a serendipitous isolation of a partial septin sequence from Ae. albopictus and its developmental expression profile. The Ae. albopictus partial septin sequence contains 591 nucleotides encoding 197 amino acids. It shares homology with several insect septin genes and has a close phylogenetic relationship with Aedes aegypti and Culex quinquefasciatus septins. The Ae. albopictus septin fragment was differentially expressed in the mosquito's developmental stages, with an increased expression in the adults.
    Matched MeSH terms: Amino Acid Sequence
  3. PARTICIPATION OF Y89 AND Y97 IN THE CONJUGATING ACTIVITY OF Drosophila melanogaster GLUTATHIONE S-TRANSFERASE D3 (DmGSTD3)
    Vignesvaran K, Alias Z
    Arch Insect Biochem Physiol, 2016 Jul;92(3):210-21.
    PMID: 27075600 DOI: 10.1002/arch.21332
    Drosophila melanogaster glutathione S-transferase D3 (DmGSTD3) has a shorter amino acid sequence as compared to other GSTs known in the fruit flies. This is due to the 15 amino acid N-terminal truncation in which normally active amino acid residue is located. The work has made use of homology modeling to visualize the arrangement of amino acid side chains in the glutathione (GSH) substrate cavity. The identified amino acids were then replaced with amino acids without functional groups in the side chains and the mutants were analyzed kinetically. Homology modeling revealed that the side chains of Y89 and Y97 were shown facing toward the substrate cavity proposing their possible role in catalyzing the conjugation. Y97A and Y89A GSH gave large changes in Km (twofold increase), Vmax (fivefold reduction), and Kcat /Km values for GSH suggesting their significant role in the conjugation reaction. The replacement at either positions has not affected the affinity of the enzyme toward 1-chloro-2,4-dinitrobenzene as no significant change in values of Kmax was observed. The replacement, however, had significantly reduced the catalytic efficiency of both mutants with (Kcat /Km )(GSH) and (Kcat /Km )(CDNB) of eight- and twofold reduction. The recombinant DmGSTD3 has shown no activity toward 1,2-dichloro-4-nitrobenzene, 2,4-hexadienal, 2,4-heptadienal, p-nitrobenzyl chloride, ethacrynic acid, and sulfobromophthalein. Therefore, it was evident that DmGSTD3 has made use of distal amino acids Y97 and Y89 for GSH conjugation.
    Matched MeSH terms: Amino Acid Sequence
  4. Fulltext Intracellular Delivery of Proteins via Fusion Peptides in Intact Plants
    Ng KK, Motoda Y, Watanabe S, Sofiman Othman A, Kigawa T, Kodama Y, et al.
    PLoS One, 2016;11(4):e0154081.
    PMID: 27100681 DOI: 10.1371/journal.pone.0154081
    In current plant biotechnology, the introduction of exogenous DNA encoding desired traits is the most common approach used to modify plants. However, general plant transformation methods can cause random integration of exogenous DNA into the plant genome. To avoid these events, alternative methods, such as a direct protein delivery system, are needed to modify the plant. Although there have been reports of the delivery of proteins into cultured plant cells, there are currently no methods for the direct delivery of proteins into intact plants, owing to their hierarchical structures. Here, we demonstrate the efficient fusion-peptide-based delivery of proteins into intact Arabidopsis thaliana. Bovine serum albumin (BSA, 66 kDa) was selected as a model protein to optimize conditions for delivery into the cytosol. The general applicability of our method to large protein cargo was also demonstrated by the delivery of alcohol dehydrogenase (ADH, 150 kDa) into the cytosol. The compatibility of the fusion peptide system with the delivery of proteins to specific cellular organelles was also demonstrated using the fluorescent protein Citrine (27 kDa) conjugated to either a nuclear localization signal (NLS) or a peroxisomal targeting signal (PTS). In conclusion, our designed fusion peptide system can deliver proteins with a wide range of molecular weights (27 to 150 kDa) into the cells of intact A. thaliana without interfering with the organelle-targeting peptide conjugated to the protein. We expect that this efficient protein delivery system will be a powerful tool in plant biotechnology.
    Matched MeSH terms: Amino Acid Sequence
  5. Fulltext Phylogenetic and Transcripts Profiling of Glucose Sensing Related Genes in Candida glabrata
    Ng TS, Mohd Desa MN, Sandai D, Chong PP, Than LT
    Jundishapur J Microbiol, 2015 Nov;8(11):e25177.
    PMID: 26855740 DOI: 10.5812/jjm.25177
    BACKGROUND: The sensing mechanism of glucose in Saccharomyces cerevisiae is well studied. However, such information is scarcely found in other yeast species such as Candida glabrata.

    OBJECTIVES: This study aimed to identify the glucose sensing pathway related genes of C. glabrata and to analyze the regulation pattern of these genes in response to different surrounding glucose concentrations through the quantitative real time polymerase chain reaction (qRT-PCR).

    MATERIALS AND METHODS: Phylogenetic analysis was carried out on predicted amino acid sequences of C. glabrata and S. cerevisiae to compare their degree of similarity. In addition, the growth of C. glabrata in response to different amounts of glucose (0%, 0.01%, 0.1%, 1% and 2%) was evaluated via the spot dilution assay on prepared agar medium. Besides, the SNF3 and RGT2, which act as putative glucose sensors, and the RGT1 and MIG1, which act as putative transcriptional regulators and selected downstream hexose transporters (HXTs), were analysed through qRT-PCR analysis for the gene expression level under different glucose concentrations.

    RESULTS: Comparative analysis of predicted amino acids in the phylogenetic tree showed high similarity between C. glabrata and S cerevisiae. Besides, C. glabrata demonstrated the capability to grow in glucose levels as low as 0.01% in the spot dilution assay. In qRT-PCR analysis, differential expressions were observed in selected genes when C. glabrata was subjected to different glucose concentrations.

    CONCLUSIONS: The constructed phylogenetic tree suggests the close evolutionary relationship between C. glabrata and S. cerevisiae. The capability of C. glabrata to grow in extremely low glucose environments and the differential expression of selected glucose-sensing related genes suggested the possible role of these genes in modulating the growth of C. glabrata in response to different glucose concentrations. This study helps deepen our understanding of the glucose sensing mechanism in C. glabrata and serves to provide fundamental data that may assist in unveiling this mechanism as a potential drug target.

    Matched MeSH terms: Amino Acid Sequence
  6. Enzyme-assisted extraction and identification of antioxidative and α-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto)
    Ngoh YY, Gan CY
    Food Chem, 2016 Jan 1;190:331-7.
    PMID: 26212978 DOI: 10.1016/j.foodchem.2015.05.120
    Antioxidant and α-amylase inhibitor peptides were successfully extracted from Pinto bean protein isolate (PBPI) using Protamex. A factorial design experiment was conducted and the effects of extraction time, pH and temperature were studied. pH 7.5, extraction time of 1h, S/E ratio of 10 (w/w) and temperature of 50 °C gave the highest antioxidant activities (i.e., ABTS scavenging activity (53.3%) and FRAP value (3.71 mM)), whereas pH 6.5 with the same extraction time, S/E ratio and temperature, gave the highest α-amylase inhibitory activity (57.5%). It was then fractioned using membrane ultrafiltration with molecular weight cutoffs of 100, 50, 30, 10 and 3 kDa. Peptide fraction <3 kDa, which exhibited the highest antioxidant activities (i.e., ABTS (42.2%) and FRAP (0.81 mM)) and α-amylase inhibitory activity (62.1%), was then subjected to LCMS and MS/MS analyses. Six sequences were identified for antioxidant peptides, whereas seven peptides for α-amylase inhibitor.
    Matched MeSH terms: Amino Acid Sequence
  7. Fulltext Molecular characterisation of new organisation of plnEF and plw loci of bacteriocin genes harbour concomitantly in Lactobacillus plantarum I-UL4
    Tai HF, Foo HL, Abdul Rahim R, Loh TC, Abdullah MP, Yoshinobu K
    Microb Cell Fact, 2015;14:89.
    PMID: 26077560 DOI: 10.1186/s12934-015-0280-y
    Bacteriocin-producing Lactic acid bacteria (LAB) have vast applications in human and animal health, as well as in food industry. The structural, immunity, regulatory, export and modification genes are required for effective bacteriocin biosynthesis. Variations in gene sequence, composition and organisation will affect the antimicrobial spectrum of bacteriocin greatly. Lactobacillus plantarum I-UL4 is a novel multiple bacteriocin producer that harbours both plw and plnEF structural genes simultaneous which has not been reported elsewhere. Therefore, molecular characterisation of bacteriocin genes that harboured in L. plantarum I-UL4 was conducted in this study.
    Matched MeSH terms: Amino Acid Sequence
  8. Cloning and sequence characterisation of falcipain-2 from Plasmodium falciparum Gombak A strain (Malaysia)
    Sim TS, Loke P, Lee MA, Singh M, Flotow H
    Parasitol Res, 2001 Sep;87(9):683-6.
    PMID: 11570549
    In this study, the genome of the Plasmodium falciparum Gombak A strain was examined for the presence of a gene encoding falcipain-2, a cysteine protease, using homology-based polymerase chain reaction cloning. The nucleotide sequence obtained from the gene cloned (designated pFG1) is approximately 99% homologous to other falcipain-2 genes from different strains. Comparatively, it is 69% homologous to falcipain-3 genes. Direct cloning of the falcipain-2 gene and its resemblance to the reported corresponding mRNA transcript suggests the absence of introns in this gene. Sequence alignment and comparison revealed four amino acid differences at positions 15, 51, 59 and 414 in the falcipain-2 from P. falciparum Gombak A as compared to other falcipain-2 proteins from different strains.
    Matched MeSH terms: Amino Acid Sequence
  9. Phylogenetic analysis of enterovirus 71 strains isolated during linked epidemics in Malaysia, Singapore, and Western Australia
    McMinn P, Lindsay K, Perera D, Chan HM, Chan KP, Cardosa MJ
    J Virol, 2001 Aug;75(16):7732-8.
    PMID: 11462047
    Enterovirus 71 (EV71) is a frequent cause of hand, foot, and mouth disease (HFMD) epidemics associated with severe neurological sequelae in a small proportion of cases. There has been a significant increase in EV71 epidemic activity throughout the Asia-Pacific region since 1997. Recent HFMD epidemics in this region have been associated with a severe form of brainstem encephalitis associated with pulmonary edema and high case fatality rates. In this study, we show that four genetic lineages of EV71 have been prevalent in the Asia-Pacific region since 1997, including two previously undescribed genogroups (B3 and B4). Furthermore, we show that viruses belonging to genogroups B3 and B4 have circulated endemically in Southeast Asia during this period and have been the primary cause of several large HFMD or encephalitis epidemics in Malaysia, Singapore, and Western Australia.
    Matched MeSH terms: Amino Acid Sequence
  10. Full length genome sequence of Tioman virus, a novel paramyxovirus in the genus Rubulavirus isolated from fruit bats in Malaysia
    Chua KB, Wang LF, Lam SK, Eaton BT
    Arch Virol, 2002 Jul;147(7):1323-48.
    PMID: 12111411
    A novel paramyxovirus in the genus Rubulavirus, named Tioman virus (TiV), was isolated in 1999 from a number of pooled urine samples of Island Flying Foxes (Pteropus hypomelanus) during the search for the reservoir host of Nipah virus. TiV is antigenically related to Menangle virus (MenV) that was isolated in Australia in 1997 during disease outbreak in pigs. Sequence analysis of the full length genome indicated that TiV is a novel member of the genus Rubulavirus within the subfamily Paramyxovirinae, family Paramyxoviridae. However, there are several features of TiV which make it unique among known paramyxoviruses and rubulaviruses in particular: (1) TiV, like MenV, uses the nucleotide G as a transcriptional initiation site, rather than the A residue used by all other known paramyxoviruses; (2) TiV uses C as the +1 residue for all intergenic regions, a feature not seen for rubulaviruses but common for all other members within the subfamily Paramyxovirinae; (3) Although the attachment protein of TiV has structural features that are conserved in other rubulaviruses, it manifests no overall sequence homology with members of the genus, lacks the sialic acid-binding motif N-R-K-S-C-S and has only two out of the six highly conserved residues known to be important for the catalytic activity of neuraminidase.
    Matched MeSH terms: Amino Acid Sequence
  11. Kernel-specific cDNA clones encoding three different isoforms of seed storage protein glutelin from oil palm Elaeis guineensis
    Cha TS, Habib Shah F
    Plant Sci, 2001 Apr;160(5):913-923.
    PMID: 11297788
    The mRNA differential display method was used to identify and isolate cDNAs corresponding to transcripts that accumulate during the period of lipid synthesis, 12-20 weeks after anthesis (WAA) in the kernel of Elaeis guineensis, var. Tenera. We successfully isolated two cDNA clones, KT7 (312 bp) and KT8 (266 bp). Interestingly, both clones show 79% nucleotide sequence identity to each other. This suggests that both clones encode the isoforms of the same protein. We screened the kernel (15 WAA) cDNA library and isolated the clone pKT7 (587 bp) using KT7 as probe, and isolated another isoform with KT8 probe, which designated as pKT9 (900 bp). Clone pKT9 has 93% nucleotide identity to KT8 and only 46% to pKT7 in their 3'-untranslated region. All three clones displayed significant amino acid sequence identity to seed storage protein glutelin from monocotyledon and globulin from dicotyledon plants. The coding sequence of KT8 (106 bp) shows 76 and 97% identity to pKT9 and pKT7, respectively. Therefore, we suggest that clones KT8 and pKT7 are members of the same subfamily (A), while pKT9 belongs to another subfamily (B) of glutelin multigene families. Southern analysis shows that there are at least four members for the subfamily B. Northern analysis shows that these three members of the glutelin family are co-ordinately expressed and developmentally regulated during the development of the kernel. The transcripts begin to accumulate at 12 WAA, increase in 15 WAA and show a significant reduction at 17 WAA.
    Matched MeSH terms: Amino Acid Sequence
  12. Revisiting the question of limited genetic variation within Schistosoma japonicum
    Le TH, Blair D, McManus DP
    Ann Trop Med Parasitol, 2002 Mar;96(2):155-64.
    PMID: 12080976
    Recent electrophoretic data have indicated that Schistosoma japonicum in mainland China may be a species complex, with the existence of a cryptic species being predicted from the analysis of schistosome populations from Sichuan province. To investigate the Sichuan form of S. japonicum, 4.9 kbp of mitochondrial DNA from each of three samples of the parasite from China (two from Sichuan and one from Hunan) and one from Sorsogon in the Philippines were amplified, sequenced and characterized. The sequence data were compared with those from the related South-east Asian species of S. mekongi (Khong Island, Laos) and S. mlayensis (Baling, Malaysia) and that from S. japonicm from Anhui (China). At both the nucleotide and amino-acid levels, the variation among the five S. japonicum samples was limited (< 1%). This was consistent with the conclusions drawn from previous molecular studies, in which minimal variation among S. japonicum populations was also detected. In contrast, S. mekongi and S. malayensis, species recognized as separate but closely related, differ from each other by about 10%, and each differs by 25%-26% from S. japonicum. Phylogenetic trees provided a graphic representation of these differences, showing all S. japonicum sequences to be very tightly clustered and distant from S. mekongi and S. malayensis, the last two being clearly distinct from each other. The results thus indicate no significant intra-specific genetic variation among S. japonicum samples collected from different geographical areas and do not support the idea of a distinct form in Sichuan.
    Matched MeSH terms: Amino Acid Sequence
  13. Sequence analysis of recent Indian isolates of foot-and-mouth disease virus serotypes O, A and Asia 1 from clinical materials
    Muthuchelvan D, Venkataramanan R, Hemadri D, Sanyal A, Tosh C
    Acta Virol., 2001 Jun;45(3):159-67.
    PMID: 11774894
    Partial nucleotide sequences of 1D gene of 38 isolates of foot-and-mouth disease virus (FMDV) of serotypes O, A and Asia 1 originating from various parts of India were determined. Field materials were subjected straight to RNA extraction, reverse transcription - PCR (RT-PCR) and sequencing. Also 3 FMDV vaccine strains, IND R2/75 (serotype O), IND 63/72 (serotype Asia 1) and IND 17/77 (serotype A) were included in the analysis. The seqences were compared mutually as well as with available corresponding sequences of other FMDV isolates, and their phylogenetic relationships were calculated. The deduced amino acid sequences showed that the serotype O isolates were relatively conserved as compared to serotype Asia 1 or A isolates from India. In phylogenetic analysis, the serotype O viruses clustered in two genotypes, one including the European vaccine strain (O1/K) and the other represented by the isolates from Bangladesh, India, Nepal and Turkey. The serotype Asia 1 viruses clustered in two groups of single genotype where the prototype strain from Pakistan (PAK 1/54) formed one group and the other was formed by the isolates from Bangladesh, Bhutan, India, Israel and Nepal. In serotype A viruses three well-differentiated genotypes were observed. The isolates from Azerbaijan, Bangladesh, Malaysia and India formed the first genotype. The second genotype was formed by isolates from Iran, Saudi Arabia and Turkey, while two recent Iranian isolates represented the third genotype. In India, the prevalence of at least one genotype could be identified in each serotype. This evolutionary clustering of isolates from the neighbor countries is not surprising, since these countries share border with India. The genetic relatedness between sequences of isolates from India and those from distant places is indicative of spread of the virus between the countries. Of importance is the fact that clinical materials proved useful for rapid generation of sequences and subsequent studying of molecular epidemiology of the disease.
    Matched MeSH terms: Amino Acid Sequence
  14. The molecular epidemiology of HIV in Asia
    Weniger BG, Takebe Y, Ou CY, Yamazaki S
    AIDS, 1994;8 Suppl 2:S13-28.
    PMID: 7857556
    Matched MeSH terms: Amino Acid Sequence
  15. Amino acid sequence similarity of Hev b 3 to two previously reported 27- and 23-kDa latex proteins allergenic to spina bifida patients
    Yeang HY, Ward MA, Zamri AS, Dennis MS, Light DR
    Allergy, 1998 May;53(5):513-9.
    PMID: 9636811
    Separate studies have reported spina bifida patients to be especially allergic to proteins of 27 and 23 kDa found in the serum of centrifuged natural rubber latex. An insoluble latex protein located on the surface of small rubber particles, Hev b 3, has similarly been found to be allergenic to spina bifida patients. In this study, internal amino acid sequences of Hev b 3 showed similarity to the published sequences for the 27- and 23-kDa latex proteins. The latter allergens are hence identified as Hev b 3. Determination of the molecular weight of Hev b 3 revealed various species of 22-23 kDa. The consistent gaps of about 266 Da observed between various forms of the intact protein suggest that the protein undergoes post-translational modification. To determine whether Hev b 3 also occurs in a soluble form in the latex serum, its presence in molecular-filtered serum was checked by ELISA and Western blot. The results showed Hev b 3 to be largely absent in the C-serum from fresh latex. The protein is therefore insoluble in its native state. However, a small amount of the solubilized protein was detected in ammonia-stabilized latex (commonly used in the manufacture of latex products).
    Matched MeSH terms: Amino Acid Sequence
  16. Identification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound protein
    To WY, Leung JC, Lai KN
    Biochim. Biophys. Acta, 1995 May 18;1249(1):58-64.
    PMID: 7766684
    We recently adopted immobilized jacalin as an affinity adsorbent to purify human serum IgA for laboratory study. In the course of our investigation, we detected a serum protein that co-eluted with IgA from jacalin-agarose affinity column. It constituted in significant quantity (24.0 +/- 0.9%, n = 30) of total jacalin-bound protein (JBP) and the yield was equivalent to 0.4 +/- 0.1 mg per ml serum. The molecular mass of this protein was 55 kDa with electromobility in the alpha 2 region as demonstrated by SDS-PAGE and immunoelectrophoresis. N-terminal microsequencing of this 55 kDa protein revealed that it is human alpha 2-HS glycoprotein (alpha 2HSG). The molecular interaction of alpha 2HSG with jacalin was characterized by competitive ELISA: human serum IgA, human colostrum secretory IgA (sIgA), and monosaccharides including D-galactose and melibiose exhibited strong inhibitory effect on its binding to jacalin. Accordingly, we propose that human alpha 2HSG binds in a similar manner as that of the bovine fetuin to jacalin. In addition, alpha 2HSG displays similar binding property to jacalin from different geographic area (India and Malaysia) and from different laboratory preparations (Sigma, Pierce and 'homemade' jacalin).
    Matched MeSH terms: Amino Acid Sequence
  17. Variation in coat protein genes among five geographically different isolates of rice tungro spherical virus
    Zhang S, Lee G, Davies JW, Hull R
    Arch Virol, 1997;142(9):1873-9.
    PMID: 9672645
    The variation in the sequence of the coat protein genes of four isolates of rice tungro spherical virus from different countries, Malaysia, Thailand, India and Bangladesh, was compared with an isolate from the Philippines. The evidence from RT-PCR, Southern blot hybridization and sequences of the coat protein genes indicated that the isolates appeared to fall into two groups. One comprised the Philippine and Malaysian isolates (about 95% sequence similarity) and the other the Bangladeshi and Indian isolates, the sequences of which differed by about 15% from that of the Philippine isolate. The Thai isolate seemed to be a mixture of these two subgroups.
    Matched MeSH terms: Amino Acid Sequence
  18. A tymovirus from Calopogonium mucunoides in Malaysia is not clitoria yellow vein tymovirus
    Gibbs AJ, Mackenzie AM, Abdul-Samad N
    Arch Virol, 1997;142(8):1697-702.
    PMID: 9672629
    A tymoyirus isolated from Malaysian crops of Calopogonium mucunoides has been shown to have virions that are serologically indistinguishable from those of clitoria yellow vein tymovirus. We have sequenced the virion protein (VP) gene of the virus and have found that although it is a member of the cluster that includes CYVV, it is the most distinct member of that cluster (< 62% sequence identity with all the others), and is clearly a separate species, which we propose should be named calopogonium yellow vein virus. Most of the serological specificity of the virions of tymoviruses seems to reside in the C-terminal hexapeptide of the virion protein.
    Matched MeSH terms: Amino Acid Sequence
  19. Sequences of the three coat protein genes of a Malaysian isolate of rice tungro spherical virus reveal a close relationship to the Philippine isolate
    Zhang S, Davies JW, Hull R
    Virus Genes, 1997;15(1):61-4.
    PMID: 9354271
    Coat protein genes CP1, CP2 and CP3 of an isolate (MaP1) of rice tungro spherical virus (RTSV) from Malaysia were isolated, cloned and sequenced. Comparative analysis indicated that MaP1 isolate is closely related to the Philippine isolate.
    Matched MeSH terms: Amino Acid Sequence
  20. Molecular evolution and epidemiology of dengue-3 viruses
    Lanciotti RS, Lewis JG, Gubler DJ, Trent DW
    J Gen Virol, 1994 Jan;75 ( Pt 1):65-75.
    PMID: 8113741
    The nucleic acid sequences of the pre-membrane/membrane and envelope protein genes of 23 geographically and temporally distinct dengue (DEN)-3 viruses were determined. This was accomplished by reverse transcriptase-PCR amplification of the structural genes followed by automated DNA sequence analysis. Comparison of nucleic acid sequences revealed that similarity among the viruses was greater than 90%. The similarity among deduced amino acids was between 95% and 100%, and in many cases identical amino acid substitutions occurred among viruses from similar geographical regions. Alignment of nucleic acid sequences followed by parsimony analysis allowed the generation of phylogenetic trees, demonstrating that geographically independent evolution of DEN-3 viruses had occurred. The DEN-3 viruses were separated into four genetically distinct subtypes. Subtype I consists of viruses from Indonesia, Malaysia, the Philippines and the South Pacific islands; subtype II consists of viruses from Thailand; subtype III consists of viruses from Sri Lanka, India, Africa and Samoa; subtype IV consists of viruses from Puerto Rico and the 1965 Tahiti virus. Phylogenetic analysis has also contributed to our understanding of the molecular epidemiology and worldwide distribution of DEN-3 viruses.
    Matched MeSH terms: Amino Acid Sequence
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