The Amino Acid Sequence of Neisseria lactamica PorB Surface-Exposed Loops Influences Toll-Like Receptor 2-Dependent Cell Activation

Toussi, Deana N.; Carraway, Margaretha; Wetzler, Lee M.; Lewis, Lisa A.; Liu, Xiuping; Massi, Paola

doi:10.1128/iai.00683-12

Cited by 25 publications

(50 citation statements)

References 64 publications

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“…5, black bar) (***, P Ͻ 0.0003, and **, P Ͻ 0.006, by a one-sample t test). Similarly, IL-8 induction by Pam 3 CSK 4 was reduced by approximately 50% or more in the presence of SB203580, SP600125, and an NF-B inhibitory ligand, while it was slightly less inhibited by U0126 (**, P Ͻ 0.002, and *, P ϭ 0.02), consistent with previous results (50). Inhibition of TNF-␣-induced IL-8 followed a similar trend, with a reduction of approximately 50% compared to TNF-␣ stimulation in the absence of inhibitors (***, P ϭ 0.0001; **, P Ͻ 0.008; and *, P ϭ 0.01).…”

Section: Resultssupporting

confidence: 81%

Toll-Like Receptor 2-Dependent Activity of Native Major Outer Membrane Protein Proteosomes of Chlamydia trachomatis

et al. 2013

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Section: Resultssupporting

confidence: 81%

Toll-Like Receptor 2-Dependent Activity of Native Major Outer Membrane Protein Proteosomes of Chlamydia trachomatis

et al. 2013

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“…The related organism Neisseria meningitidis also possesses a porB gene which shares 60 to 70% amino acid sequence homology with gonococcal porB. Like the gonococcus, meningococcal PorB also inhibits apoptosis induction and can modulate immune responses via binding to and inducing signaling downstream of Toll-like receptor 2 (25)(26)(27)(28)(29)(30)(31).…”

mentioning

confidence: 99%

Structure-Function Studies of the Neisseria gonorrhoeae Major Outer Membrane Porin

Chen

Seifert

2013

Infect Immun

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The major outer membrane porin (PorB) expressed by Neisseria gonorrhoeae plays multiple roles during infection, in addition to its function as an outer membrane pore. We have generated a panel of mutants of N. gonorrhoeae strain FA1090 expressing a variety of mutant porB genes that all function as porins. We identified multiple regions of porin that are involved in its binding to the complement regulatory factors C4b-binding protein and factor H and confirmed that the ability to bind at least one factor is required for FA1090 to survive the bactericidal effects of human serum. We tested the ability of these mutants to inhibit both apoptosis and the oxidative burst in polymorphonuclear leukocytes but were unable to identify the porin domains required for either function. This study has identified nonessential porin domains and some potentially essential portions of the protein and has further expanded our understanding of the contribution of the porin domains required for complement regulation.

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“…NL strain Y92-1009 (ND:P1.ND,ND:F-ND:ST-3493, ST-613), NM serogroup B strain H44/76 (B:15;P1.7,16; L3,7,9, ST-32) Δ1Δ4 variant (lacking expression of PorA and Rmp), and the NM mutant strain expressing PorB from NL (NM-[ Nlac PorB]) [24] were cultured from frozen stocks on GC agar plates containing 1% Isovitalex at 37°C in a 5% CO 2 atmosphere in candle jars. The next day, colonies were resuspended in GC liquid medium containing 1% Isovitalex and grown for approx.…”

Section: Methodsmentioning

confidence: 99%

“…the laminin receptor LamR [21], the gp96 and Scavenger Receptor SREC [14]), with complement components [22] and with members of the Toll-like receptor family, specifically TLR2 and TLR1 [23]. Residues that likely mediate PorB/TLR2 interaction and subsequent host cell activation have been identified in the surface-exposed regions of loops 5 and 7 of PorB [24]. …”

Section: Introductionmentioning

confidence: 99%

Neisseriae internalization by epithelial cells is enhanced by TLR2 stimulation

Toussi

Wetzler

Liu

et al. 2016

Microbes and Infection

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N. meningitidis (NM) is an opportunistic gram-negative human pathogen that colonizes the human nasopharyngeal epithelium. Asymptomatic carriage is common, but some meningococcal strains can invade nasopharyngeal epithelial cells and proceed to cause severe and often fatal infections. Invasion is predominantly driven by expression of bacterial virulence factors and host cell cognate receptors for bacterial recognition. Porins are among the Neisserial components involved in host cell activation and bacterial internalization processes. Similar to other virulence factors, porins present antigenic and structure variability among strains. Such sequence variability in the surface-exposed loop regions has been correlated to bacterial invasiveness and to variability in host cell responses via Toll-like receptor 2 (TLR2). Here, we examined whether TLR2 signaling by porins influences recovery of intracellular Neisseriae from epithelial cells in vitro. Our results show that TLR2 stimulation, either by the organism or exogenously, generally enhances Neisseriae internalization by epithelial cells. TLR2-driven intracellular signaling via ERK1/2, JNK and particularly NF-κB plays a role in this process. Based on these results, it is possible that expression of porin sequence variants that strongly induce TLR2 activation may be a mechanism to enhance the invasive features of pathogenic Neisseriae strains.

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The Amino Acid Sequence of Neisseria lactamica PorB Surface-Exposed Loops Influences Toll-Like Receptor 2-Dependent Cell Activation

Cited by 25 publications

References 64 publications

Toll-Like Receptor 2-Dependent Activity of Native Major Outer Membrane Protein Proteosomes of Chlamydia trachomatis

Toll-Like Receptor 2-Dependent Activity of Native Major Outer Membrane Protein Proteosomes of Chlamydia trachomatis

Structure-Function Studies of the Neisseria gonorrhoeae Major Outer Membrane Porin

Neisseriae internalization by epithelial cells is enhanced by TLR2 stimulation

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