2019
DOI: 10.1080/19490976.2019.1602428
|View full text |Cite
|
Sign up to set email alerts
|

Serine-rich repeat proteins from gut microbes

Abstract: Serine-rich repeat proteins (SRRPs) have emerged as an important group of cell surface adhesins found in a growing number of Gram-positive bacteria. Studies focused on SRRPs from streptococci and staphylococci demonstrated that these proteins are O-glycosylated on serine or threonine residues and exported via an accessory secretion (aSec) system. In pathogens, these adhesins contribute to disease pathogenesis and represent therapeutic targets. Recently, the non-canonical aSec system has been identified in the … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
26
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
5
3
2

Relationship

0
10

Authors

Journals

citations
Cited by 26 publications
(26 citation statements)
references
References 87 publications
0
26
0
Order By: Relevance
“…The history of this hydrophilic amino acid and its essential involvement in the pathogenesis of SARS-CoV-2 strongly suggest that the binding between pathogen and host occurs via O-glycosylation. Although serine-rich repeat proteins (SRRPs) that are involved in the adhesion of different bacteria (Latousakis et al, 2020) to host cell carbohydrates via O-glycosylation have not yet been described for the pathogenesis of viral infections, such a mechanism might occur in the pathogenesis of SARS-CoV infections. Moreover, the inhibition of the TMPRSS2 enzyme or the blocking of serine mobilization, studied by Meyer et al (2013) in an E. coli infection, might be utilized by newer pharmaceuticals in future therapeutic strategies against SARS-CoV-2 (Wang et al, 2020).…”
Section: Proposed Blood Group-independent and Abo(h) Blood Groupspecimentioning
confidence: 99%
“…The history of this hydrophilic amino acid and its essential involvement in the pathogenesis of SARS-CoV-2 strongly suggest that the binding between pathogen and host occurs via O-glycosylation. Although serine-rich repeat proteins (SRRPs) that are involved in the adhesion of different bacteria (Latousakis et al, 2020) to host cell carbohydrates via O-glycosylation have not yet been described for the pathogenesis of viral infections, such a mechanism might occur in the pathogenesis of SARS-CoV infections. Moreover, the inhibition of the TMPRSS2 enzyme or the blocking of serine mobilization, studied by Meyer et al (2013) in an E. coli infection, might be utilized by newer pharmaceuticals in future therapeutic strategies against SARS-CoV-2 (Wang et al, 2020).…”
Section: Proposed Blood Group-independent and Abo(h) Blood Groupspecimentioning
confidence: 99%
“…The serine-rich repeat proteins (SRRPs) are common on the surface of various lactobacilli such as Limosilactobacillus reuteri , but none of them have been found in the genome of L. plantarum [ 58 ]. Further studies will be needed to explain this curious pattern of tRNA-Ser expression in L. plantarum Ym1 under butanol stress.…”
Section: Resultsmentioning
confidence: 99%
“…The history of this hydrophilic amino acid and its essential involvement in the pathogenesis of SARS-CoV-2 strongly suggest that the binding between pathogen and host occurs via O -glycosylation. Although serine-rich repeat proteins (SRRPs) that are involved in the adhesion of different bacteria ( Latousakis et al, 2020 ) to host cell carbohydrates via O -glycosylation have not yet been described for the pathogenesis of viral infections, such a mechanism might occur in the pathogenesis of SARS-CoV infections. Moreover, the inhibition of the TMPRSS2 enzyme or the blocking of serine mobilization could be therapeutic strategies against the influenza virus ( Meyer et al, 2013 ) and SARS-CoV-2 ( Wang et al, 2020 ).…”
Section: Proposed Blood Group-independent and Abo(h) Blood Group-specmentioning
confidence: 99%