نتایج جستجو برای: ompa outer membrane protein

تعداد نتایج: 1527767  

Journal: :Journal of bacteriology 1994
D N Collier

Signal peptides of gram-positive exoproteins generally carry a higher net positive charge at their amino termini (N regions) and have longer hydrophobic cores (h regions) and carboxy termini (C regions) than do signal peptides of Escherichia coli envelope proteins. To determine if these differences are functionally significant, the ability of Bacillus subtilis to secrete four different E. coli ...

Journal: :modares journal of medical sciences: pathobiology 2014
kobra ahmadi zanoos iraj rasooli abolfazl jahangiri mohammad reza rahbar shakiba darvish alipour astaneh

objectives: acinetobacter baumannii is a gram-negative, non-motile aerobic bacterium known as a nosocomial pathogen resisting often to broad range of antibiotics. the pathogen is a serious agent of mortality and morbidity in hospital particularly among immunocompromise patients. treatment and control of its infections is complicated owing to its high antibiotic resistance, survival in various e...

Journal: :Journal of bacteriology 2014
Luis David Ginez Aurora Osorio Sebastian Poggio

The outer membrane of Gram-negative bacteria is an essential structure involved in nutrient uptake, protection against harmful substances, and cell growth. Different proteins keep the outer membrane from blebbing out by simultaneously interacting with it and with the cell wall. These proteins have been mainly studied in enterobacteria, where OmpA and the Braun and Pal lipoproteins stabilize the...

2017
Pascal Rainard Maryline Répérant-Ferter Christophe Gitton Florence B Gilbert Pierre Germon

The outer membrane protein (Omp) A is a major constituent of the outer membrane of Escherichia coli. This protein has been used in several vaccine development studies, but seldom with a view to vaccinating against mastitis. The objective of this study was to investigate the immunogenicity of E. coli OmpA and its vaccine potential for cows. Both the humoral and cellular immune responses were inv...

Journal: :Applied and environmental microbiology 2006
Michelle L Power Belinda C Ferrari Jane Littlefield-Wyer David M Gordon Martin B Slade Duncan A Veal

A novel Escherichia coli outer membrane protein A (OmpA) was discovered through a proteomic investigation of cell surface proteins. DNA polymorphisms were localized to regions encoding the protein's surface-exposed loops which are known phage receptor sites. Bacteriophage sensitivity testing indicated an association between bacteriophage resistance and isolates having the novel ompA allele.

Journal: :The new microbiologica 2010
Stefania Starnino Rosanna Leuzzi Valeria Ghisetti Maria Antonia De Francesco Marco Cusini Giampaolo Impara Emma Galluppi Mariagrazia Pizza Paola Stefanelli

Molecular analyses of mip and ompA genes were performed on 20 Neisseria gonorrhoeae isolates. The genes were present with a high degree of conservation in all strains. Sera from patients with urethritis or disseminated gonococcal infections were able to recognize the purified Neisseria gonorrhoeae macrophage infectivity potentiator (Ng-MIP) and Neisseria gonorrhoeae outer membrane protein A (Ng...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2009
Troy A Walton Cristina M Sandoval C Andrew Fowler Arthur Pardi Marcelo C Sousa

Outer membrane proteins (OMPs) of gram-negative bacteria are synthesized in the cytosol and must cross the periplasm before insertion into the outer membrane. The 17-kDa protein (Skp) is a periplasmic chaperone that assists the folding and insertion of many OMPs, including OmpA, a model OMP with a membrane embedded beta-barrel domain and a periplasmic alphabeta domain. Structurally, Skp belongs...

Journal: :Biophysical journal 2017
Firdaus Samsudin Alister Boags Thomas J Piggot Syma Khalid

Gram-negative bacteria such as Escherichia coli are protected by a complex cell envelope. The development of novel therapeutics against these bacteria necessitates a molecular level understanding of the structure-dynamics-function relationships of the various components of the cell envelope. We use atomistic MD simulations to reveal the details of covalent and noncovalent protein interactions t...

Journal: :Infection and immunity 1990
R Puohiniemi M Karvonen J Vuopio-Varkila A Muotiala I M Helander M Sarvas

We produced in Bacillus subtilis the complete, as well as the N-terminal two-thirds, OmpA protein of Escherichia coli (called here Bac-OmpA and Bac-OmpA-dN, respectively). These Bac-OmpA proteins were used to examine the immunological properties of different parts of OmpA, free of lipopolysaccharide and other components of the outer membrane. The full-length Bac-OmpA was indistinguishable from ...

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