A New Tandem Repeat in Bovine Fibrinogen Aα Gene

Inaba, Yumi; Tsurifune, K.; Sasazaki, Shinji; Mannen, Hideyuki

doi:10.1080/10495390801929122

Cited by 2 publications

(3 citation statements)

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“…The enhanced binding affinity of Srr2 was linked with increased adherence to endothelial cells, which may be important for Group B Streptococcus -associated meningitis [49]. The ability of the Srr and SpsL proteins to adhere to more than one site in the tandem repeat region of the fibrinogen α-chain may have evolved as a mechanism for overcoming extant genetic diversity in this region between individuals within a host species as observed in the current study for SpsL (Fig 4G) [39, 50].…”

Section: Discussionmentioning

confidence: 74%

“…The number of tandem repeats in the bovine fibrinogen α-chain have been reported to differ between cattle breeds [39]. To investigate if this is also the case for dogs we investigated publicly available canine sequences of the fibrinogen α-chain but, due to the repetitive nature of the tandem repeat region, the paired-end short sequence reads were not sufficient to support assembly and robust analysis.…”

Section: Resultsmentioning

confidence: 99%

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Host-specialized fibrinogen-binding by a bacterial surface protein promotes biofilm formation and innate immune evasion

et al. 2019

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Fibrinogen is an essential part of the blood coagulation cascade and a major component of the extracellular matrix in mammals. The interface between fibrinogen and bacterial pathogens is an important determinant of the outcome of infection. Here, we demonstrate that a canine host-restricted skin pathogen, Staphylococcus pseudintermedius , produces a cell wall-associated protein (SpsL) that has evolved the capacity for high strength binding to canine fibrinogen, with reduced binding to fibrinogen of other mammalian species including humans. Binding occurs via the surface-expressed N2N3 subdomains, of the SpsL A-domain, to multiple sites in the fibrinogen α-chain C-domain by a mechanism analogous to the classical dock, lock, and latch binding model. Host-specific binding is dependent on a tandem repeat region of the fibrinogen α-chain, a region highly divergent between mammals. Of note, we discovered that the tandem repeat region is also polymorphic in different canine breeds suggesting a potential influence on canine host susceptibility to S . pseudintermedius infection. Importantly, the strong host-specific fibrinogen-binding interaction of SpsL to canine fibrinogen is essential for bacterial aggregation and biofilm formation, and promotes resistance to neutrophil phagocytosis, suggesting a key role for the interaction during pathogenesis. Taken together, we have dissected a bacterial surface protein-ligand interaction resulting from the co-evolution of host and pathogen that promotes host-specific innate immune evasion and may contribute to its host-restricted ecology.

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Section: Discussionmentioning

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Host-specialized fibrinogen-binding by a bacterial surface protein promotes biofilm formation and innate immune evasion

et al. 2019

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“…Additional Staphylococcal CWA proteins demonstrate a more host-specialized fibrinogen interaction with the repeat region of the fibrinogen α-chain, which exhibits both inter-and intraspecies variation (Murakawa et al, 1993;Inaba et al, 2008;Pickering et al, 2019). For example, clumping factor B (ClfB) of S. aureus interacts solely with repeat 5 of the human fibrinogen α-chain, promoting human-specialized platelet aggregation, with S. pseudintermedius surface protein L (SpsL) exhibiting caninespecialized high-affinity binding to the repeat region of the canine fibrinogen α-chain (Miajlovic et al, 2007;Walsh et al, 2008;Pickering et al, 2019).…”

Section: Staphylococcal Interactions With Fibrinogenmentioning

confidence: 99%

The Role of Gram-Positive Surface Proteins in Bacterial Niche- and Host-Specialization

Pickering

Fitzgerald

2020

Front. Microbiol.

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Gram-positive bacterial pathogens have an array of proteins on their cell surface that mediate interactions with the host environment. In particular, bacterial cell wallassociated (CWA) proteins play key roles in both colonization and pathogenesis. Furthermore, some CWA proteins promote specialization for host-species or mediate colonization of specific anatomical niches within a host. In this mini review, we provide examples of the many ways by which major pathogens, such as Staphylococci, Streptococci and Listeria monocytogenes, utilize CWA proteins for both host-and niche-specialization. We describe different biological mechanisms mediated by CWA proteins including: the acquisition of iron from hemoglobin in the bloodstream, adherence to and invasion of host cells, and innate immune evasion through binding to the plasma proteins fibrinogen, immunoglobulin G, and complement. We also discuss the limitations of using animal models for understanding the role of specific CWA proteins in host-specialization and how transformative technologies, such as CRISPR-Cas, offer tremendous potential for developing transgenic models that simulate the host environment of interest. Improved understanding of the role of CWA proteins in nicheor host-specificity will allow the design of new therapeutic approaches which target key host-pathogen interactions underpinning Gram-positive bacterial infections.

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A New Tandem Repeat in Bovine Fibrinogen Aα Gene

Cited by 2 publications

References 11 publications

Host-specialized fibrinogen-binding by a bacterial surface protein promotes biofilm formation and innate immune evasion

Host-specialized fibrinogen-binding by a bacterial surface protein promotes biofilm formation and innate immune evasion

The Role of Gram-Positive Surface Proteins in Bacterial Niche- and Host-Specialization

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