Pseudomonas aeruginosa CRASP-2 is a surface protein that uses the human terminal complement regulator vitronectin for protection against complement-mediated attack

Hallstroem, Teresia; Uhde, Melanie; Mörgelin, Matthias; Skerka, Christine; Zipfel, Peter F.

doi:10.1016/j.molimm.2010.05.121

Cited by 4 publications

(2 citation statements)

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“…Both types of strains activate complement cascades equally; the remarkable property of resistant strains is the reduced insertion of C5b-9 in the membrane and hence results in increased survival (Schiller and Joiner, 1986). In a more recent report, P. aeruginosa complement regulator-acquiring surface proteins (CRASP-2) showed direct binding to Vn heparin-binding domains and inhibited the complement mediated lysis (Hallström et al, 2010).…”

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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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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“…VTN is also known to bind to a number of different bacteria. In the cases of Haemophilus influenzae [ 147 ], Moraxella catarrhalis [ 148 ] and Pseudomonas aeruginosa [ 149 ], VTN binding inhibits MAC formation. Neisseria meningitidis [ 150 ] and Neisseria gonorrheae [ 151 ] also bind VTN, but whether this is to avoid complement activation has yet to be determined.…”

Section: Extracellular Chaperones (Ecs) Implicated In Complement Regu...mentioning

confidence: 99%

The Emerging Roles of Extracellular Chaperones in Complement Regulation

Geraghty

Satapathy

Wilson

2022

Cells

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The immune system is essential to protect organisms from internal and external threats. The rapidly acting, non-specific innate immune system includes complement, which initiates an inflammatory cascade and can form pores in the membranes of target cells to induce cell lysis. Regulation of protein homeostasis (proteostasis) is essential for normal cellular and organismal function, and has been implicated in processes controlling immunity and infection. Chaperones are key players in maintaining proteostasis in both the intra- and extracellular environments. Whilst intracellular proteostasis is well-characterised, the role of constitutively secreted extracellular chaperones (ECs) is less well understood. ECs may interact with invading pathogens, and elements of the subsequent immune response, including the complement pathway. Both ECs and complement can influence the progression of neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and amyotrophic lateral sclerosis, as well as other diseases including kidney diseases and diabetes. This review will examine known and recently discovered ECs, and their roles in immunity, with a specific focus on the complement pathway.

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Vitronectin binding protein, BOM1093, confers serum resistance on Borrelia miyamotoi

Sato

Kumagai

Sekizuka

et al. 2021

Sci Rep

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Borrelia miyamotoi, a member of the tick-borne relapsing fever spirochetes, shows a serum-resistant phenotype in vitro. This ability of B. miyamotoi may contribute to bacterial evasion of the host innate immune system. To investigate the molecular mechanism of serum-resistance, we constructed a membrane protein-encoding gene library of B. miyamotoi using Borrelia garinii strain HT59G, which shows a transformable and serum-susceptible phenotype. By screening the library, we found that bom1093 and bom1515 of B. miyamotoi provided a serum-resistant phenotype to the recipient B. garinii. These B. miyamotoi genes are predicted to encode P35-like antigen genes and are conserved among relapsing fever borreliae. Functional analysis revealed that BOM1093 bound to serum vitronectin and that the C-terminal region of BOM1093 was involved in the vitronectin-binding property. Importantly, the B. garinii transformant was not serum-resistant when the C terminus-truncated BOM1093 was expressed. We also observed that the depletion of vitronectin from human serum enhances the bactericidal activity of BOM1093 expressing B. garinii, and the survival rate of BOM1093 expressing B. garinii in vitronectin-depleted serum is enhanced by the addition of purified vitronectin. Our data suggests that B. miyamotoi utilize BOM1093-mediated binding to vitronectin as a mechanism of serum resistance.

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Pseudomonas aeruginosa CRASP-2 is a surface protein that uses the human terminal complement regulator vitronectin for protection against complement-mediated attack

Cited by 4 publications

References 0 publications

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

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

The Emerging Roles of Extracellular Chaperones in Complement Regulation

Vitronectin binding protein, BOM1093, confers serum resistance on Borrelia miyamotoi

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