Immune evasion of the human pathogenic yeast Candida albicans: Pra1 is a Factor H, FHL-1 and plasminogen binding surface protein

Luo, Shanshan; Poltermann, Sophia; Kunert, Anja; Rupp, Steffen; Zipfel, Peter F.

doi:10.1016/j.molimm.2009.07.017

Cited by 99 publications

(111 citation statements)

References 48 publications

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“…Factor H and FHL-1 are recruited by bacterial and fungal complement regulator-acquiring surface proteins and are attached via the same domains, that is, SCRs 6-7 and SCRs 18-20. Microbial proteins that bind Factor H and FHL-1 via these domains include Rck from Salmonella enterica and Gpm1 and Pra1 from C. albicans (23,35,44,45). A second group of microbial surface proteins binds the two human regulators either via SCRs 6-7 (e.g., M proteins and Fba from Streptococcus pyogenes, NspA from Neisseria meningitidis, CRASP-1 from B. burgdorferi) or via SCRs 18-20 (e.g., Scl1 from S. pyogenes and Por1B from Neisseria gonorrheae) of Factor H (30,(46)(47)(48).…”

Section: Discussionmentioning

confidence: 99%

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Dihydrolipoamide Dehydrogenase of Pseudomonas aeruginosa Is a Surface-Exposed Immune Evasion Protein That Binds Three Members of the Factor H Family and Plasminogen

Hallström

Mörgelin

Barthel

et al. 2012

The Journal of Immunology

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The opportunistic human pathogen Pseudomonas aeruginosa causes a wide range of diseases. To cross host innate immune barriers, P. aeruginosa has developed efficient strategies to escape host complement attack. In this study, we identify the 57-kDa dihydrolipoamide dehydrogenase (Lpd) as a surface-exposed protein of P. aeruginosa that binds the four human plasma proteins, Factor H, Factor H-like protein-1 (FHL-1), complement Factor H-related protein 1 (CFHR1), and plasminogen. Factor H contacts Lpd via short consensus repeats 7 and 18–20. Factor H, FHL-1, and plasminogen when bound to Lpd were functionally active. Factor H and FHL-1 displayed complement-regulatory activity, and bound plasminogen, when converted to the active protease plasmin, cleaved the chromogenic substrate S-2251 and the natural substrate fibrinogen. The lpd of P. aeruginosa is a rather conserved gene; a total of 22 synonymous and 3 nonsynonymous mutations was identified in the lpd gene of the 5 laboratory strains and 13 clinical isolates. Lpd is surface exposed and contributes to survival of P. aeruginosa in human serum. Bacterial survival was reduced when Lpd was blocked on the surface prior to challenge with human serum. Similarly, bacterial survival was reduced up to 84% when the bacteria was challenged with complement active serum depleted of Factor H, FHL-1, and CFHR1, demonstrating a protective role of the attached human regulators from complement attack. In summary, Lpd is a novel surface-exposed virulence factor of P. aeruginosa that binds Factor H, FHL-1, CFHR1, and plasminogen, and the Lpd-attached regulators are relevant for innate immune escape and most likely contribute to tissue invasion.

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Section: Discussionmentioning

confidence: 99%

“…Several microbial Factor H-binding proteins also bind plasminogen (34)(35)(36)(37). We therefore asked whether P. aeruginosa Lpd also binds plasminogen.…”

Section: Lpd Binds Human Plasminogenmentioning

confidence: 99%

Dihydrolipoamide Dehydrogenase of Pseudomonas aeruginosa Is a Surface-Exposed Immune Evasion Protein That Binds Three Members of the Factor H Family and Plasminogen

Hallström

Mörgelin

Barthel

et al. 2012

The Journal of Immunology

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“…Several invasive human pathogens bind plasminogen, including Streptococcus pneumoniae (21), S. aureus (22), Pseudomonas aeruginosa (23), Haemophilus influenzae (24), Helicobacter pylori (25), and the yeast Candida albicans (26,27). Several B. burgdorferi plasminogen-binding proteins have been identified, such as the infection-associated surface proteins CspA (complement regulator-acquiring surface protein 1; CRASP-1) and CspZ (CRASP-2) (28), ErpP (CRASP-3), ErpC (CRASP-4), ErpA (CRASP-5) (29), the 70-kDa surface protein BPBP (30), OspA (31), and OspC, which a recent study, employing live cell binding assays, has shown to be a plasminogen receptor on the surface of B. burgdorferi (32,33).…”

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confidence: 99%

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Koenigs

Hammerschmidt

Jutras

et al. 2013

Journal of Biological Chemistry

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Background: Recruitment of plasminogen is important for efficient dissemination of Borrelia burgdorferi. Results: BBA70 of B. burgdorferi binds plasminogen, and following activation, bound plasmin can cleave fibrinogen and inactivate the key complement components C3b and C5. Conclusion: BBA70 is a potent plasminogen-binding protein.Significance: Investigation suggests that binding of plasminogen may aid in pathogen dissemination and inhibit bacteriolytic effects of the host complement system.

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“…In addition, C. albicans via the surface protein Gpm1 was shown to bind host vitronectin, thereby mediating adhesion to epithelial cells . Furthermore, C. albicans phosphoglycerat mutase 1 and pH-regulated antigen 1 were shown to bind Factor-H, FHL-1 and plasminogen (Poltermann et al, 2007;Luo et al, 2009). Besides, the expression levels of Gpm1/pH-regulated antigen 1 were shown to increase fungal survival in the presence of serum and increased adhesion to endothelial cells (Luo et al, 2015).…”

Section: Serum Factorsmentioning

confidence: 99%

Fungal sensing of host environment

Braunsdorf

Mailänder-Sánchez²,

Schaller

2016

Cellular Microbiology

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Summary To survive inside a host, fungi have to adapt to a changing and often hostile environment and therefore need the ability to recognize what is going on around them. To adapt to different host niches, they need to sense external conditions such as temperature, pH and to recognize specific host factors. The ability to respond to physiological changes inside the host, independent of being in a commensal, pathogenic or even symbiotic context, implicates mechanisms for sensing of specific host factors. Because the cell wall is constantly in contact with the surrounding, fungi express receptors on the surface of their cell wall, such as pheromone receptors, which have important roles, besides mediating chemotropism for mating. We are not restricting the discussion to the human host because the receptors and mechanisms used by different fungal species to sense their environment are often similar even for plant pathogens. Furthermore, the natural habitat of opportunistic pathogenic fungi with the potential to cause infection in a human host is in soil and on plants. While the hosts' mechanisms of sensing fungal pathogens have been addressed in the literature, the focus of this review is to fill the gap, giving an overview on fungal sensing of a host‐(ile) environment. Expanding our knowledge on host–fungal interactions is extremely important to prevent and treat diseases of pathogenic fungi, which are important issues in human health and agriculture but also to understand the delicate balance of fungal symbionts in our ecosystem.

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Immune evasion of the human pathogenic yeast Candida albicans: Pra1 is a Factor H, FHL-1 and plasminogen binding surface protein

Cited by 99 publications

References 48 publications

Dihydrolipoamide Dehydrogenase of Pseudomonas aeruginosa Is a Surface-Exposed Immune Evasion Protein That Binds Three Members of the Factor H Family and Plasminogen

Dihydrolipoamide Dehydrogenase of Pseudomonas aeruginosa Is a Surface-Exposed Immune Evasion Protein That Binds Three Members of the Factor H Family and Plasminogen

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Fungal sensing of host environment

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