Identification of a Novel Streptococcal Adhesin P (SadP) Protein Recognizing Galactosyl-α1–4-galactose-containing Glycoconjugates

Kouki, Annika; Haataja, Sauli; Loimaranta, Vuokko; Pulliainen, Arto T.; Nilsson, Ulf J.; Finne, Jukka

doi:10.1074/jbc.m111.260992

Cited by 40 publications

(56 citation statements)

References 70 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We demonstrated that SadP1 contributes to the adhesion to human IEC by binding of Gb3/CD77 confirming previous functional studies on recombinant galabiose-binding N-terminal domain of SadP recognizing Gb3/CD77 as its natural glycolipid host-cell receptor [11, 47]. Recent studies on the structure of SadP1 in interaction with Gb2, which is analogous to Gb3/CD77, identified 10 AA critical for binding of SadP1 to the homologous structure of galabiose of Gb2 [47].…”

Section: Discussionsupporting

confidence: 88%

“…Analysis of SadP binding specificity to galabiose present in the Gbs receptors revealed the highest specificity to the globotriaosylceramide Gb3/CD77 receptor [11]. Gb3/CD77 receptors are abundant in various host tissues including human and pig small intestine in the precursor (Gb3/CD77) or mature form (globotetraosylceramide Gb4) [13, 14].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium

et al. 2017

View full text Add to dashboard Cite

BackgroundStreptococcus suis is a zoonotic pathogen, causing meningitis and septicemia. We previously demonstrated that the gastrointestinal tract (GIT) is an entry site for zoonotic S. suis infection. Here we studied the contribution of Streptococcal adhesin Protein (SadP) to host-pathogen interaction at GIT level.MethodsSadP expression in presence of Intestinal Epithelial Cells (IEC) was compared with expression of other virulence factors by measuring transcript levels using quantitative Real Time PCR (qRT-PCR). SadP variants were identified by phylogenetic analysis of complete DNA sequences. The interaction of SadP knockout and complementation mutants with IEC was tested in vitro.ResultsExpression of sadP was significantly increased in presence of IEC. Sequence analysis of 116 invasive strains revealed five SadP sequence variants, correlating with genotype. SadP1, present in zoonotic isolates of clonal complex 1, contributed to binding to both human and porcine IEC and translocation across human IEC. Antibodies against the globotriaosylceramide Gb3/CD77 receptor significantly inhibited adhesion to human IEC.ConclusionSadP is involved in the host-pathogen interaction in the GIT. Differences between SadP variants may determine different affinities to the Gb3/CD77 host-receptor, contributing to variation in adhesion capacity to host IEC and thus to S. suis zoonotic potential.

show abstract

Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Suilysin, the extracellular protein factor, along with a muramidase-released protein have also been shown to be linked to, but not essential for, the full virulence of S. suis [21]. GapdH [22], Enolase [23], [24], Fibronectin/Fibrinogen-binding protein [25], HAM1 [26] and Adhesion [27], [28], [29], [30], [31], [32] have been shown to be involved in S. suis adherence and virulence. Serum opacity-like factor [33], D-Alanylation of Lipoteichoic Acid [34], Peptidoglycan GlcNAc deacetylase [35], IgA protease [36], [37], TroA [38], SodA [39], SsFHB [40] and Subtilisin-like serine protease [41], [42], [43] are also considered to be related to S. suis virulence.…”

Section: Introductionmentioning

confidence: 99%

HP0197 Contributes to CPS Synthesis and the Virulence of Streptococcus suis via CcpA

et al. 2012

View full text Add to dashboard Cite

Streptococcus suis serotype 2 (SS2), a major swine pathogen and an emerging zoonotic agent, has greatly challenged global public health. The encoding proteins with unknown functions the bacterium encodes are an obstruction to studies of the pathogenesis. A novel surface protective antigen HP0197 is one of these proteins which have no sequence homology to any known protein. In the present study, the protein was determined to be involved in bacterial virulence through an evaluation of the isogenic mutant (Δhp0197) in both mice and pigs. The experimental infection also indicated that Δhp0197 could be cleared easily during infection, which could be attributed to the reduced thickness of the capsular polysaccharides (CPS) and the significantly reduced phagocytotic resistance. Microarrays-based comparative transcriptome analysis suggested that the suppressed expression of the operon responsible for CPS synthesis might be reversed by CcpA activity, which controlled global regulation of carbon catabolite through the binding of the CcpA and HPr-Ser-46-P to the catabolite-responsive elements (cre) of the target operons. The hypothesis was approved by the fact that the purified FLAG-tagged HPr from WT stain exhibited a higher binding activity to cre with CcpA compared to the Δhp0197 by the Electrophoretic Mobility Shift Assay, suggesting lower level of phosphorylation of the phosphocarrier protein HPr at residue Ser-46 (HPr-Ser-46P) in Δhp0197. These indicated that HP0197 could enhance CcpA activity to control the expression of genes involved in carbohydrate utilization and CPS synthesis, thus contributing to the virulence of S. suis.

show abstract

“…The isolates differed by an inserted region, with genes which were likely inserted as a whole, but the origin of this inserted sequence is not well understood. The isolates also had different SadP genes, previously characterized as an adhesin as well as a factor H binding protein which may contribute to zoonotic potential (Ferrando et al, ) and is considered a putative virulence factor of S. suis (Kouki et al, ; Pian et al, ).…”

Section: Discussionmentioning

confidence: 99%

Reinfection with Streptococcus suis analysed by whole genome sequencing

Willemse

Ende

Schultsz

2018

Zoonoses and Public Health

View full text Add to dashboard Cite

A butcher with chronic dermatitis presented with a second episode of Streptococcus suis meningitis, 8 years after the first episode. To distinguish between reinfection and persistent carriage, we compared the two S. suis isolates using whole genome sequencing. We investigated whole genome sequences of the S. suis isolates by means of substitution rates and population structure of closely related strains in addition to available clinical information. Genome‐wide analyses revealed an inserted region consisting of 12 genes in the first isolate and the calculated substitution rate between the isolates suggested infections were caused by highly similar, but unrelated strains. Continuous occupational exposure likely resulted in reinfection with S. suis in a butcher.

show abstract

Identification of a Novel Streptococcal Adhesin P (SadP) Protein Recognizing Galactosyl-α1–4-galactose-containing Glycoconjugates

Cited by 40 publications

References 70 publications

Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium

Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium

HP0197 Contributes to CPS Synthesis and the Virulence of Streptococcus suis via CcpA

Reinfection with Streptococcus suis analysed by whole genome sequencing

Contact Info

Product

Resources

About