scholarly journals The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning β-barrel

2015 ◽  
Vol 35 (4) ◽  
Author(s):  
Adam Dyer ◽  
Gemma Brown ◽  
Lenka Stejskal ◽  
Peter R. Laity ◽  
Richard J. Bingham
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Human Factor ◽  
Factor H ◽  
Size Exclusion ◽  
Scattering Data ◽  
Borrelia Afzelii ◽  
Monomeric Structure ◽  
Membrane Spanning

We present the characterization of BAPKO_0422, an outer membrane protein from Borrelia afzelii. Circular dichroism, size exclusion and small angle X-ray scattering data indicate a monomeric structure rich in β-strand. Recombinant BAPKO_0422 binds to human factor H.

Contribution of the outer membrane protein OmpW in Escherichia coli to complement resistance from binding to factor H

2016 ◽  
Vol 98 ◽  
pp. 57-62 ◽  
Author(s):  
Weiyan Li ◽  
Liangyou Wen ◽  
Chuchu Li ◽  
Ran Chen ◽  
Zhicang Ye ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Factor H ◽  
Complement Resistance

scholarly journals TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability

2005 ◽  
Vol 187 (18) ◽  
pp. 6499-6508 ◽  
Author(s):  
Karsten R. O. Hazlett ◽  
David L. Cox ◽  
Marc Decaffmeyer ◽  
Michael P. Bennett ◽  
Daniel C. Desrosiers ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Nutrient Transport ◽  
Treponema Pallidum ◽  
Protein S ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Membrane Spanning

ABSTRACT The outer membrane of Treponema pallidum, the noncultivable agent of venereal syphilis, contains a paucity of protein(s) which has yet to be definitively identified. In contrast, the outer membranes of gram-negative bacteria contain abundant immunogenic membrane-spanning β-barrel proteins mainly involved in nutrient transport. The absence of orthologs of gram-negative porins and outer membrane nutrient-specific transporters in the T. pallidum genome predicts that nutrient transport across the outer membrane must differ fundamentally in T. pallidum and gram-negative bacteria. Here we describe a T. pallidum outer membrane protein (TP0453) that, in contrast to all integral outer membrane proteins of known structure, lacks extensive β-sheet structure and does not traverse the outer membrane to become surface exposed. TP0453 is a lipoprotein with an amphiphilic polypeptide containing multiple membrane-inserting, amphipathic α-helices. Insertion of the recombinant, nonlipidated protein into artificial membranes results in bilayer destabilization and enhanced permeability. Our findings lead us to hypothesize that TP0453 is a novel type of bacterial outer membrane protein which may render the T. pallidum outer membrane permeable to nutrients while remaining inaccessible to antibody.

Duck Complement Factor H Binds to Outer Membrane Protein Omp24 of Riemerella anatipestifer

2021 ◽  
Vol 65 (2) ◽  
Author(s):  
Delong Li ◽  
Xiangli Wang ◽  
Xingsheng Xu ◽  
Jiulong Gu ◽  
Yunchuan Yang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Riemerella Anatipestifer

scholarly journals Outer Membrane Protein P5 Is Required for Resistance of Nontypeable Haemophilus influenzae to Both the Classical and Alternative Complement Pathways

2013 ◽  
Vol 82 (2) ◽  
pp. 640-649 ◽  
Author(s):  
Charles V. Rosadini ◽  
Sanjay Ram ◽  
Brian J. Akerley
Keyword(s):  
Membrane Protein ◽  
Haemophilus Influenzae ◽  
Outer Membrane ◽  
Outer Surface ◽  
Outer Membrane Protein ◽  
Alternative Pathway ◽  
Factor H ◽  
Classical Pathway ◽  
Surface Binding ◽  
Content Type

ABSTRACTThe complement system is an important first line of defense against the human pathogenHaemophilus influenzae. To survive and propagatein vivo,H. influenzaehas evolved mechanisms for subverting this host defense, most of which have been shown to involve outer surface structures, including lipooligosaccharide glycans and outer surface proteins. Bacterial defense against complement acts at multiple steps in the pathway by mechanisms that are not fully understood. Here we identify outer membrane protein P5 as an essential factor in serum resistance of bothH. influenzaestrain Rd and nontypeableH. influenzae(NTHi) clinical isolate NT127. P5 was essential for resistance of Rd and NT127 to complement in pooled human serum. Further investigation determined that P5 expression decreased cell surface binding of IgM, a potent activator of the classical pathway of complement, to both Rd and NT127. Additionally, P5 expression was required for NT127 to bind factor H (fH), an important inhibitor of alternative pathway (AP) activation. Collectively, the results obtained in this work highlight the ability ofH. influenzaeto utilize a single protein to perform multiple protective functions for evading host immunity.

scholarly journals Prediction of the membrane-spanning β-strands of the major outer membrane protein of Chlamydia

2009 ◽  
Vol 11 (7) ◽  
pp. 1854-1861 ◽  
Author(s):  
María José Rodríguez-Marañón ◽  
Robin M. Bush ◽  
Ellena M. Peterson ◽  
Tilman Schirmer ◽  
Luis M. de la Maza
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Major Outer Membrane Protein ◽  
Membrane Spanning
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