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1.
JMB-Journal of Medical Bacteriology. 2012; 1 (2): 53-61
in English | IMEMR | ID: emr-139766

ABSTRACT

Staphylococcus aureus is a major human pathogen worldwide. Vancomycin has been used for decades to treat multidrug resistant S. aureus. Ten years has passed since the first report of vancomycin resistant S. aureus [VRSA]. The objective of this systematic review was to determine the total number of VRSA isolates that have been reported from Iran. Search terms reflected [Iran], [vancomycin] and [SI aureus] were searched in the ISI web of knowledge, PubMed, SciVerse, and Google scholar. Also two Persian scientific databases and 13 recent national congresses were investigated. Articles / abstracts working on S. aureus in Iran, evaluating vancomycin MIC and / or PCR of vanA/B were included in this systematic review. Out of the 3484 records found in mentioned resources, 13 related studies were included in the final analysis. The result showed that at least 24 VRSA isolates which have been reported from Iran up to September 2012. It seems that many Iranian researchers did not follow a spe-cific guideline for reporting and confirming VRSA. Establishing an Iranian reference center where studies on VRSA can be registered, evaluat-ed and confirmed is strongly recommended


Subject(s)
Humans , Male , Female , Drug Resistance, Microbial , Staphylococcus aureus/drug effects , Anti-Bacterial Agents/pharmacology , Polymerase Chain Reaction
2.
AJMB-Avicenna Journal of Medical Biotechnology. 2011; 3 (4): 207-210
in English | IMEMR | ID: emr-127843

ABSTRACT

Expressions of recombinant proteins for different applications are important objectives in molecular biotechnology; however, expression of some recombinant proteins is difficult. Several methods have been designed for expression of these proteins. The aim of this study was to construct a vector containing Mtb32C fragment of Mycobacterium tuberculosis [M.tuberculosis] as a fusion partner in order to improve the expression of fused recombinant proteins. Mtb32C was amplified by polymerase chain reaction [PCR]. The amplified fragment was ligated into pET21b+ vector. Colony-PCR, enzyme digestion and DNA sequencing methods were used to confirm the recombinant vector. Colony-PCR showed a 420 bp fragment in size corresponding to the correct size of our fragment. In addition the recombinant plasmids sequencing showed the accuracy of the cloned fragment. For confirming the expression, reverse transcriptase [RT]-PCR analysis was performed showing a 420 bp fragment in agarose gel electrophoresis using specific primers. The construction of a vector containing Mtb32C fragment is promising as a fusion partner for future studies as it affected the expression of the fused proteins and increased immune responses against the partner

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