The role of porins in neisserial pathogenesis and immunity

Massi, Paola; Ram, Sanjay; MacLeod, Heather; Wetzler, Lee M.

doi:10.1016/s0966-842x(02)00037-9

Cited by 160 publications

(108 citation statements)

References 56 publications

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…However, additional TLR2 ligands do not require TLR1 or TLR6 for signaling, implying that TLR2 recognizes some ligands as a homodimer or heterodimer with other non-TLR molecules. Such TLR2 ligands include the Gram-positive cell wall component lipoteichoic acid; the mycobacterial cell wall component lipoarabinomannan; atypical LPS produced by Legionella, Leptospira interrogans, Porphyromonas gingivitis and Bordetella; and porins present in the outer membrane of Neisseria (Massari et al, 2003;Wetzler, 2003).…”

Section: Bacterial Recognitionmentioning

confidence: 99%

NF-κB and the immune response

2006

View full text Add to dashboard Cite

Section: Bacterial Recognitionmentioning

confidence: 99%

NF-κB and the immune response

2006

View full text Add to dashboard Cite

“…Both N. meningitidis and N. gonorrhoeae PorB [60% identical; (4,5)] are believed to contribute to disease progression (6). During infection, PorB targets to the mitochondria (7,8) where it likely inserts into the inner membrane (9).…”

mentioning

confidence: 99%

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

Tanabe

Nimigean²,

Iverson³

2010

Proc. Natl. Acad. Sci. U.S.A.

110

View full text Add to dashboard Cite

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 Å 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.antibiotic resistance | innate immunity | outer membrane protein | porin | selectivity

show abstract

“…Class 1 outer membrane protein (PorA) is a major component of the outer membrane of Neisseria meningitidis and functions as a cationic porin [17]. Previous studies have shown that PorA is immunogenic during natural infection and is also a target for bactericidal antibodies, following immunization with experimental OMVs [18,19].…”

Section: Discussionmentioning

confidence: 99%

Cloning, expression and purification of outer membrane protein PorA of Neisseria meningitidis serogroup B

Haghi

Peerayeh

Siadat

et al. 2011

J Infect Dev Ctries

View full text Add to dashboard Cite

Introduction: Neisseria meningitidis is a major causative agent of bacterial septicemia and meningitis in humans. Currently, there are no vaccines to prevent disease caused by strains of N. meningitidis serogroup B. PorA is a major component of the outer membrane of N. meningitidis and functions as a cationic porin. This study aimed to clone and determine the expression of PorA. Methodology: A 1200 bp fragment of porA gene was amplified by PCR from serogroup B N. meningitidis and then cloned into prokaryotic expression vector pET-32a. For expression of recombinant protein, pET32a-porA plasmid was transformed into competent Origami B (DE3) cells. Recombinant protein was overexpressed with isopropythio-beta-D-galctoside (IPTG) and affinity purified by Ni-NTA agarose. SDS-PAGE and western blotting were performed for protein determination and verification. Results: Cloning of porA was confirmed by colony-PCR and enzymatic digestion. In comparison with the corresponding sequences of original genes, the nucleotide sequence homology of the cloned porA gene was 97%. IPTG with a dosage of 1.0 mmol/L could efficiently induce protein expression. SDS-PAGE analysis showed that our constructed prokaryotic expression system pET32a-PorA-Origami efficiently produces a target recombinant protein with a molecular weight of 65 kDa. The recombinant PorA was overexpressed as inclusion bodies and reacted with the serum from a rabbit previously immunized with native outer membrane vesicle. Conclusion: This prokaryotic expression system provides an easy method for producing recombinant PorA and may also be useful for the production of other bacterial outer membrane proteins for vaccine studies.

show abstract

The role of porins in neisserial pathogenesis and immunity

Cited by 160 publications

References 56 publications

NF-κB and the immune response

NF-κB and the immune response

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

Cloning, expression and purification of outer membrane protein PorA of Neisseria meningitidis serogroup B

Contact Info

Product

Resources

About