NDLI: Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition

Content Provider	PubMed Central
Author	Kattner, Christof Deana, Toussi Zaucha, Jan Wetzler, Lee M. Nadine, Rüppel Zachariae, Ulrich Massari, Paola Tanabe, Mikio
Copyright Year	2013
Abstract	Among all Neisseriae species, N. meningitidis and N. gonorrhoeae are the only human pathogens, causative agents of bacterial meningitis and gonorrhoea, respectively. PorB, a pan-Neisseriae trimeric porin that mediates diffusive transport of essential molecules across the bacterial outer membrane, is also known to activate host innate immunity via Toll-like receptor 2 (TLR2)-mediated signaling. The molecular mechanism of PorB binding to TLR2 is not known, but it has been hypothesized that electrostatic interactions contribute to ligand/receptor binding. Strain-specific sequence variability in the surface-exposed loops of PorB which are potentially implicated in TLR2 binding, may explain the difference in TLR2-mediated cell activation in vitro by PorB homologs from the commensal N. lactamica and the pathogen N. meningitidis. Here, we report a comparative structural analysis of PorB from N. meningitidis serogroup B strain 8765 (63% sequence homology with PorB from N. meningitidis serogroup W135) and a mutant in which amino acid substitutions in the extracellular loop 7 lead to significantly reduced TLR2-dependent activity in vitro. We observe that this mutation both alters the loop conformation and causes dramatic changes of electrostatic surface charge, both of which may affect TLR2 recognition and signalling.
Related Links	http://dx.doi.org/10.1016/j.jsb.2013.12.006
Ending Page	447
Page Count	8
Starting Page	440
File Format	PDF
ISSN	10478477
e-ISSN	10958657
Journal	Journal of structural biology
Issue Number	3
Volume Number	185
Language	English
Publisher Date	2014-03-01
Access Restriction	Open
Subject Keyword	Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology

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