Glycosylation and biogenesis of a family of serine-rich bacterial adhesins.
Meixian Zhou,Hui Wu +1 more
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TLDR
This review examines a new family of serine-rich O-linked glycoproteins which are represented by fimbriae-associated adhesin Fap1 of Streptococcus parasanguinis and human platelet-binding protein GspB of StrePTococcus gordonii and proposes a two-step glycosylation model.Abstract:
Glycosylation of bacterial proteins is an important process for bacterial physiology and pathophysiology. Both O- and N-linked glycan moieties have been identified in bacterial glycoproteins. The N-linked glycosylation pathways are well established in Gram-negative bacteria. However, the O-linked glycosylation pathways are not well defined due to the complex nature of known O-linked glycoproteins in bacteria. In this review, we examine a new family of serine-rich O-linked glycoproteins which are represented by fimbriae-associated adhesin Fap1 of Streptococcus parasanguinis and human platelet-binding protein GspB of Streptococcus gordonii. This family of glycoproteins is conserved in streptococcal and staphylococcal species. A gene cluster coding for glycosyltransferases and accessory Sec proteins has been implicated in the protein glycosylation. A two-step glycosylation model is proposed. Two glycosyltransferases interact with each other and catalyse the first step of the protein glycosylation in the cytoplasm; the cross-talk between glycosylation-associated proteins and accessory Sec components mediates the second step of the protein glycosylation, an emerging mechanism for bacterial O-linked protein glycosylation. Dissecting the molecular mechanism of this conserved biosynthetic pathway offers opportunities to develop new therapeutic strategies targeting this previously unrecognized pathway, as serine-rich glycoproteins have been shown to play a role in bacterial pathogenesis.read more
Citations
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Streptococcus Adherence and Colonization
TL;DR: There is much focus on applying increasingly advanced molecular techniques to determine the precise structures and functions of these proteins, and their regulatory pathways, so that more targeted approaches can be developed against streptococcal infections.
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Biology of Oral Streptococci.
Jacqueline Abranches,Lin Zeng,Jessica K. Kajfasz,Sara R. Palmer,Brinta Chakraborty,Zezhang T. Wen,Vincent P. Richards,L. J. Brady,José A. Lemos +8 more
TL;DR: The different oral environments inhabited by streptococci and the species that occupy each niche are discussed, with special attention to the taxonomy of Streptococcus, which is now divided into eight distinct groups.
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Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes.
TL;DR: It is shown how the OST-mediated N- and O-glycosylation pathways share cytoplasmic assembly of lipid-linked oligosaccharides, flipping across the ER/periplasmic/cytop lasmic membranes, and transferring “en bloc” to the protein acceptor, which are mirrored in lipopolysaccharide biosynthesis.
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The Pneumococcal Serine-Rich Repeat Protein Is an Intra-Species Bacterial Adhesin That Promotes Bacterial Aggregation In Vivo and in Biofilms
Carlos J. Sanchez,Pooja Shivshankar,Kim Stol,Samuel Trakhtenbroit,Paul M. Sullam,Karin Sauer,Peter W. M. Hermans,Carlos J. Orihuela +7 more
TL;DR: The first report to show the presence of biofilm-like structures in the lungs of animals infected with S. pneumoniae is reported and recombinant Non-repeat domains of SRRPs may be useful as vaccine antigens to protect against Gram-positive bacteria that cause infection.
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The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells.
TL;DR: It is concluded that the BR domain of PsrP binds to K10 in a lectin‐independent manner, that K10 is expressed on lung cells and that vaccination with rPsrPBR is protective against pneumococcal disease.
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