METHODS: Cross-sectional study was conducted from Jun 2018 to May 2019. Isolates from first-positive peripheral blood cultures were tested with Prolex Staph Xtra Latex agglutination test, together with routine tube coagulase and DNase test. All isolates were further confirmed with Vitek2 GP.
RESULTS: Hundred isolates were tested with Prolex Staph Xtra Latex. Twelve isolates were excluded due to incomplete medical records. Eighty-eight isolates were analysed, yielded sensitivities, specificities, positive and negative predictive values of 100%, 91.7%, 98.7%, and 100%, respectively. Of these, 76 were identified as S. aureus and 12 CoNS. Seventy-six patients were included in the SAB analysis. Fifty-nine out of 76 (78.6%) had underlying comorbidities. Thirty-four percent of the episodes were considered as primary SAB. Skin and soft tissue infection were accounted for the highest source of bacteraemia, 24(31.6%). Both MRSA and MSSA bacteraemia were seen mostly among healthcare-associated bacteraemia (HCA) (7/16, 43.8% and 28/60, 46.7%). Liver cirrhosis was significantly associated with MRSA bacteraemia (P=0.048). Metastatic infection & complicated SAB were identified in 13(17.1%) and 30(39.5%) of cases, respectively. All-cause mortality was 22.4%.
CONCLUSION: S. aureus bacteraemia is a serious infection associated with significant metastatic complications and mortality. Prolex Staph Xtra Latex agglutination test has excellent sensitivity and specificity with 100% and 91.7% respectively.
OBJECTIVE: Based on their biological capability, various acetogenins were studied in the present study and compared alongside ABT-737 on molecular docking.
METHODS: The docking simulation of acetogenins was performed using AutoDock Vina software.
RESULTS: Our findings have shown eleven acetogenins-BCL-XL protein complex, namely, muricin B (2), muricin F (4), muricin H (6), muricin I (7), xylomaticin (9), annomontacin (12), annonacin (14), squamocin (15), squamostatin A (16), bullatacin (20) and annoreticulin (21) exhibited strong binding affinities lower than - 10.4 kcalmol-1 as compared to ABT-373-BCL-XL complex. Six hydrogen bonds along with hydrophobic interaction were detected on the complex of BCL-XL with muricin B (2), muricin G (5), corossolone (11), and isoannonacin-10-one A (18).
CONCLUSION: These findings indicated that some acetogenins could represent a new potential BCLXL inhibitor that could mimic the BH3-only protein for the induction of apoptosis in cancer chemotherapy.