Department of Anesthesiology

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Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.

TitleStructural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB.
Publication TypeJournal Article
Year of Publication2010
AuthorsTanabe M, Nimigean CM, Iverson TM
JournalProc Natl Acad Sci U S A
Volume107
Issue15
Pagination6811-6
Date Published2010 Apr 13
ISSN1091-6490
KeywordsAnions, Bacterial Outer Membrane Proteins, Biological Transport, Carbohydrates, Crystallography, X-Ray, Humans, Immunity, Innate, Liposomes, Models, Molecular, Molecular Conformation, Neisseria meningitidis, Nucleotides, Porins, Toll-Like Receptors
Abstract

PorB is the second most prevalent outer membrane protein in Neisseria meningitidis. PorB is required for neisserial pathogenesis and can elicit a Toll-like receptor mediated host immune response. Here, the x-ray crystal structure of PorB has been determined to 2.3 A resolution. Structural analysis and cocrystallization studies identify three putative solute translocation pathways through the channel pore: One pathway transports anions nonselectively, one transports cations nonselectively, and one facilitates the specific uptake of sugars. During infection, PorB likely binds host mitochondrial ATP, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates these translocation pathways both by partial occlusion of the pore and by restricting the motion of a putative voltage gating loop. PorB is located on the surface of N. meningitidis and can be recognized by receptors of the host innate immune system. Features of PorB suggest that Toll-like receptor mediated recognition outer membrane proteins may be initiated with a nonspecific electrostatic attraction.

DOI10.1073/pnas.0912115107
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID20351243
PubMed Central IDPMC2872391
Grant ListGM079419 / GM / NIGMS NIH HHS / United States
GM081816 / GM / NIGMS NIH HHS / United States
R01 GM077560-06 / GM / NIGMS NIH HHS / United States
R01 GM079419-04 / GM / NIGMS NIH HHS / United States
RR-01646 / RR / NCRR NIH HHS / United States