Binding of S protein by Neisseria gonorrhoeae and potential role in invasion

Arko, R J; Chen, Cheng‐Yen; Schalla, W. O.; Sarafian, S. K.; Taylor, Calli; Knapp, Joan S.; Morse, S. A.

doi:10.1128/jcm.29.1.70-75.1991

Cited by 15 publications

(10 citation statements)

References 24 publications

(27 reference statements)

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“…suggesting a direct interaction (Arko et al, 1991); this interaction is unlikely to involve Opc as N. gonorrhoeae do not express the protein. A more recent study described that the nVn was more effective than polymeric (activated) Vn in the indirect heparin-dependent N. gonorrhoeae binding to Vn through the expression of certain Opa adhesins.…”

Section: Haemostasis Vitronectin Activation and Its Harnessing By Mementioning

confidence: 98%

“…However, specific targeting of soluble aVn and importance in serum resistance has been less well recognized. Interestingly, early studies on Neisseria gonorrhoeae (Arko et al, 1991) suggested that aVn may be required for gonococcal Vn-mediated serum survival. Although the mechanism of Vn binding was not known, gonococcal attachment to Vn was not affected by heparin A and B. MAC deposition and serum survival of capsulate MC58 (A and B) or H44/76 MsfB16++Dopc (C and D) in 10% PHS supplemented as shown were determined as described in Experimental procedures.…”

Section: Haemostasis Vitronectin Activation and Its Harnessing By Mementioning

confidence: 99%

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Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance

Griffiths¹,

Hill²,

Borodina³

et al. 2011

Molecular Microbiology

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SummaryComplement evasion is an important survival strategy of Neisseria meningitidis (Nm) during colonization and infection. Previously, we have shown that Nm Opc binds to serum vitronectin to inhibit complementmediated killing. In this study, we demonstrate meningococcal interactions with vitronectin via a novel adhesin, Msf (meningococcal surface fibril, previously NhhA or Hsf). As with Opc, Msf binds preferentially to activated vitronectin (aVn), engaging at its N-terminal region but the C-terminal heparin binding domain may also participate. However, unlike Opc, the latter binding is not heparin-mediated. By binding to aVn, Msf or Opc can impart serum resistance, which is further increased in coexpressers, a phenomenon dependent on serum aVn concentrations. The survival fitness of aVn-binding derivatives was evident from mixed population studies, in which msf/opc mutants were preferentially depleted. In addition, using vitronectin peptides to block Msf-aVn interactions, aVninduced inhibition of lytic C5b-9 formation and of serum killing could be reversed. As Msf-encoding gene is ubiquitous in the meningococcal strains examined and is expressed in vivo, serum resistance via Msf may be of significance to meningococcal pathogenesis. The data imply that vitronectin binding may be an important strategy for the in vivo survival of Nm for which the bacterium has evolved redundant mechanisms.

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Section: Haemostasis Vitronectin Activation and Its Harnessing By Mementioning

confidence: 98%

Section: Haemostasis Vitronectin Activation and Its Harnessing By Mementioning

confidence: 99%

Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance

Griffiths¹,

Hill²,

Borodina³

et al. 2011

Molecular Microbiology

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“…The majority of the DGI isolates (n = 35; 92%) were highly serum resistant together with their Vn-binding capacity in comparison with septic joint and CSF isolates. Intriguingly, Vn binding was suggested as the major factor in survival and serum resistance of DGI isolates of N. gonorrhoeae (Arko et al, 1991).…”

Section: Figmentioning

confidence: 99%

Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion

Singh

Riesbeck³

2010

Molecular Microbiology

177

238

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SummaryThe multifunctional human glycoprotein vitronectin (Vn) plays a significant role in cell migration, tissue repair and regulation of membrane attack complex (MAC) formation. It also promotes neutrophil infiltration and, thus, enhances the inflammatory process during infection. In the host, a balanced homeostasis is maintained by Vn due to neutralization of the selfreactivity of the MAC. On the other hand, Vn bound to the bacterial surface protects from MAC-mediated lysis and enhances adhesion. Gram-negative bacterial pathogens including Moraxella catarrhalis, Haemophilus influenzae and Neisseria gonorrhoeae use Vn recruitment to prevent MAC deposition at their surface. Moreover, Gram-positive bacterial pathogens such as Streptococcus pneumoniae and S. pyogenes utilize Vn for effective adhesion to host cells and subsequent internalization. Vitronectin has an ArgGly-Asp (RGD) sequence for binding the host cell integrin receptors and a separate bacterial-binding domain for pathogens, and thus more likely functions to cross-link bacteria and epithelial cells. Once bacteria are attached to the vitronectin-integrin complex, various host cell-signalling events are activated and promote internalization. In this review, we focus on the important roles of vitronectin in bacterial pathogenesis and describe different strategies used by pathogens to evade the host response by the help of this intriguing molecule.

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“…Vitronectin has previously been shown to interact with the surface of several bacterial species, including Escherichia coli, Staphylococcus aureus, streptococci, Pneumocystis carinii, and Neisseria meningitidis (7,15,16,32), and it has been shown to promote agglutination of gonococci (2). In N. meningitidis, the acquisition of vitronectin increases the adherence of this bacterium to human umbilical vein endothelial cells (32).…”

Section: Figmentioning

confidence: 99%

Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells

Duensing

Putten

1997

Infect Immun

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Gonococci producing a distinct opacity protein (OpaA in strain MS11) adhere to and are efficiently internalized by cultured epithelial cells such as the Chang conjunctiva cell line. Both adherence and uptake require interactions between OpaA and heparan sulfate proteoglycans on the mammalian cell surface. Chinese hamster ovary (CHO) cells also support adherence of gonococci through interactions of OpaA with cell surface heparan sulfate proteoglycans. However, despite this similarity in the requirements for adherence, CHO cells are not capable of internalizing gonococci. In this report, we characterized this apparent deficiency and identified a factor in fetal calf serum (FCS) which is capable of mediating uptake of gonococci by CHO cells. In the absence of FCS, OpaA ؉ gonococci adhered to but were not internalized by CHO cells, whereas in the presence of up to 15% FCS, the bacteria were efficiently internalized by the cells. Preincubation of bacteria, but not cells, with FCS also stimulated internalization, suggesting that a factor present in FCS was binding to the surface of gonococci and subsequently stimulating entry. Using a combination of chromatographic purification procedures, we identified the adhesive glycoprotein vitronectin as the serum factor which mediates the internalization of gonococci by CHO cells. Vitronectin-depleted serum did not support gonococcal entry, and this deficiency was restored by the addition of purified vitronectin. Further experiments using a set of gonococcal recombinants, each expressing a single member of the family of Opa outer membrane proteins, demonstrated that vitronectin bound to the surface of OpaA-producing gonococci only and that the vitronectinmediated uptake by the CHO cells was limited to this bacterial phenotype. To our knowledge, our data are the first example that vitronectin can serve as a molecule that drives bacterial entry into epithelial cells.

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Binding of S protein by Neisseria gonorrhoeae and potential role in invasion

Cited by 15 publications

References 24 publications

Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance

Meningococcal surface fibril (Msf) binds to activated vitronectin and inhibits the terminal complement pathway to increase serum resistance

Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion

Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells

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