PENICILLIN BINDING PROTEINS (PBPs) IN HAEMOPHILUS INFLUENZAE (HI)
نویسندگان
چکیده
منابع مشابه
Analysis of penicillin-binding proteins (PBPs) in carbapenem resistant Acinetobacter baumannii
BACKGROUND & OBJECTIVES Acinetobacter baumannii is a Gram-negative, cocco-bacillus aerobic pathogen responsible for nosocomial infections in hospitals. In the recent past A. baumannii had developed resistance against β-lactams, even against carbapenems. Penicillin-binding proteins (PBPs) are crucial for the cell wall biosynthesis during cell proliferation and these are the target for β-lactams....
متن کاملHaemophilus Influenzae B
یکی از شایع ترین مننژیت باکتریایی در شیرخواران، هموفیلوس آنفلوانزا از نوع B (HIB) می باشد. به منظور تهیه و عرضه واکسنی جهت حفظ کودکان در مقابل این بیماری به بازار جهانی، تحقیقاتی انجام و نوعی واکسن در بخش تحقیقاتی آکسفورد مورد آزمایش و ارزیابی قرار گرفت تا در صورت تمایل والدین و کارکنان بهداشتی، تجویز همزمان آن با واکسن سه گانه و فلج اطفال عملی گردد.
متن کاملDocking and Molecular Modelling of the Target - Penicillin Binding Protein -1A of Haemophilus influenzae
Penicillin binding protein-1A (PBP-1A; IPR011816) plays a pivotal role in the biogenesis of cell-wall and biosynthesis of peptidoglycan in bacteria. It is considered to be a novel target for pneumonia. The present study is to deduce the structure of the PBP-1A using ICM Molsoft and to validate the same with Ramachandran plot. These bioinformatics tools have been used to identify a lead molecule...
متن کاملCloning of conserved regions of nontypeable Haemophilus influenzae hmw1 core binding domain
Colonization of nontypeable Haemophilus influenzae (NTHi) in nasopharynx causes respiratory tract disease. In 80% of clinical isolates, HMW proteins are the major adhesions and induce protective antibodies in the hosts. Therefore, it can be used as a vaccine candidate. The aim of this study is designing and cloning of the conserved regions of NTHi hmw1 core binding domain.In this study, the sta...
متن کاملBinding of human hemoglobin by Haemophilus influenzae.
Binding of biotinylated human hemoglobin to Haemophilus influenzae was detected when organisms were grown in heme-deplete, but not heme-replete, conditions. Hemoglobin binding was completely inhibited by a 100-fold excess of unlabelled human hemoglobin or human hemoglobin complexed with human haptoglobin. Binding was only partially inhibited by rat hemoglobin, bovine hemoglobin, human globin, a...
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ژورنال
عنوان ژورنال: Pediatric Research
سال: 1984
ISSN: 0031-3998,1530-0447
DOI: 10.1203/00006450-198404001-01130