Adherence and internalization of Streptococcus gordonii by epithelial cells involves ?1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides

Nobbs, Angela H.; Shearer, Barbara; Drobni, Mirva; Jepson, Mark A.; Jenkinson, Howard F.

doi:10.1111/j.1462-5822.2006.00768.x

Cited by 55 publications

(53 citation statements)

References 84 publications

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“…AgI/II family polypeptides have been shown to play important roles in host colonization by facilitating binding interactions with epithelial cell surfaces (30,51,52). The ability of the archetypal Bsp family member BspA to facilitate binding to vaginal epithelial cells when presented on the surface of nonadherent bacterium L. lactis suggests a role for BspA, and perhaps other Bsp proteins, in facilitating host cell adherence and colonization.…”

Section: Discussionmentioning

confidence: 99%

Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae

Rego

Heal

Pidwill

et al. 2016

Journal of Biological Chemistry

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Streptococcus agalactiae (group B Streptococcus, GBS) is the predominant cause of early-onset infectious disease in neonates and is responsible for life-threatening infections in elderly and immunocompromised individuals. Clinical manifestations of GBS infection include sepsis, pneumonia, and meningitis. Here, we describe BspA, a deviant antigen I/II family polypeptide that confers adhesive properties linked to pathogenesis in GBS. Heterologous expression of BspA on the surface of the non-adherent bacterium Lactococcus lactis confers adherence to scavenger receptor gp340, human vaginal epithelium, and to the fungus Candida albicans. Complementary crystallographic and biophysical characterization of BspA reveal a novel ␤-sandwich adhesion domain and unique asparagine-dependent super-helical stalk. Collectively, these findings establish a new bacterial adhesin structure that has in effect been hijacked by a pathogenic Streptococcus species to provide competitive advantage in human mucosal infections. Streptococcus agalactiae (group B Streptococcus (GBS)4 ) is a commensal of the gastrointestinal tract and part of the normal microbiota of the female rectovaginal tract, where it is carried asymptomatically by ϳ10 -40% of women of childbearing age (1). However, as an opportunistic pathogen, GBS is the leading cause of neonatal meningitis and sepsis in the developed world. The predominant route by which GBS is transmitted to infants is from the mother, either during birth or following breach of the placental barrier in utero. Antenatal GBS screening strategies are therefore commonly used to identify colonized women, who then receive antimicrobial prophylaxis. Nevertheless, GBS remains a major cause of morbidity and mortality in infants worldwide (2).Because maternal GBS colonization is the primary risk factor for vertical transmission of neonatal infection (3), there has been considerable focus on the mechanisms underlying GBS colonization of the female genitourinary (GU) tract. A number of putative colonization determinants have been identified, including the following: ␣C protein, mediating entry of GBS into cervical epithelial cells (4); pili, shown to contribute to vaginal attachment (5); and Srr-1, which binds keratin-4 (5) and fibrinogen (6) on the surface of vaginal epithelium. In addition, GBS expresses numerous extracellular matrix-binding proteins, including C5a peptidase (ScpB) and FbsA, which may promote attachment to mucosal tissues of the GU tract (7).Antigen I/II (AgI/II) family polypeptide adhesins are found widely across the Streptococcus genus and have been best characterized for those streptococci indigenous to the oral cavity (8). In silico analyses have recently revealed the presence of genes encoding AgI/II family polypeptides in GBS, which we have designated here group B Streptococcus surface proteins (Bsp). These proteins conform to a conserved primary structure consisting of seven distinct regions (Fig. 1). The N-terminal region comprises a signal (leader) peptide, an N-terminal domain, and an ...

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Section: Discussionmentioning

confidence: 99%

Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae

Rego

Heal

Pidwill

et al. 2016

Journal of Biological Chemistry

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“…The antigen I/II family of proteins are ubiquitous to streptococci being found in most published genomes to date with roles in the development of microbial communities and adhesion to host cells and proteins [57]. Like the SRR proteins they share a common domain organisation: a signal sequence; an N-terminal region; an alanine rich repeat domain; a variable domain; a proline rich repeat region; a C-terminal region and a cell wall anchor domain [58].…”

Section: Antigen I/ii Family Of Bacterial Adhesinsmentioning

confidence: 99%

“…SspA and SspB participate in fluid phase interactions with salivary glycoprotein gp340, facilitating bacterial clumping which most likely aids in the development of biofilms [59,60]. Additionally, they mediate adherence and internalisation into epithelial cells via β1 intregins [57], can bind to collagen type 1 [61] and interact with other oral microorganisms: Candida albicans [62]; Porphyromonas gingivalis [63]; and Actinomyces naeslundii [60]. Given their critical role in induction of platelet aggregation it is tempting to speculate that S. gordonii strains lacking antigen I/II proteins may have reduced virulence in IE due to failure to propagate platelet activation.…”

Section: Antigen I/ii Family Of Bacterial Adhesinsmentioning

confidence: 99%

Platelet-Bacterial Interactions in the Pathogenesis of Infective Endocarditis — Part I: The Streptococcus

Tilley¹,

Steven²

2013

Recent Advances in Infective Endocarditis

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“…The antigen I/II family of proteins are probably the best characterised proteins on the surface of S. gordonii. Originally identified on Streptococcus mutans, antigen I/II have now been identified on almost all oral streptococci (Nobbs et al, 2007). In S. gordonii, antigen I/II have been designated SspA/B.…”

Section: Platelet-bacterial Interactions: the Streptococcusmentioning

confidence: 99%

“…In S. gordonii, antigen I/II have been designated SspA/B. These proteins are oligospecific adhesins which have been shown to bind to several ligands such as collagen type I (Heddle et al, 2003), β 1 integrins (Nobbs et al, 2007), salivary agglutinin glycoprotein (Prakobphol et al, 2000) as well as other bacteria including P. gingivalis, Candida albicans and Actinomyces naeslundii (Demuth et al, 2001;Egland et al, 2001;Jakubovics et al, 2005b). Deletion of SspA/B from S. gordonii DL1 failed to affect either platelet aggregation or platelet adhesion.…”

Section: Platelet-bacterial Interactions: the Streptococcusmentioning

confidence: 99%

Platelet-Bacterial Interactions as Therapeutic Targets in Infective Endocarditis

Kerrigan¹,

Cox²

2012

Endocarditis

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Adherence and internalization of Streptococcus gordonii by epithelial cells involves ?1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides

Cited by 55 publications

References 84 publications

Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae

Structural and Functional Analysis of Cell Wall-anchored Polypeptide Adhesin BspA in Streptococcus agalactiae

Platelet-Bacterial Interactions in the Pathogenesis of Infective Endocarditis — Part I: The Streptococcus

Platelet-Bacterial Interactions as Therapeutic Targets in Infective Endocarditis

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