The changing faces of <i>Streptococcus</i> antigen I/II polypeptide family adhesins

Brady, L. Jeannine; Maddocks, Sarah; Larson, Matthew R.; Forsgren, Nina; Persson, Karina; Deivanayagam, Champion; Jenkinson, Howard F.

doi:10.1111/j.1365-2958.2010.07212.x

Cited by 153 publications

(210 citation statements)

References 70 publications

(104 reference statements)

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“…Our proposed role of the BspA-V domain in target binding is consistent with studies of other AgI/II family polypeptides, where the V domain has been identified as a major determinant of adherence (8). The crystal structure of the BspA-V domain demonstrates that this domain adopts a fold that is distinct from those reported for other AgI/II family polypeptides, comprising an elaborated ␤-sandwich core, which exposes a sizeable binding pocket at the interface of its two constituent ␤-sheets.…”

Section: Discussionsupporting

confidence: 88%

“…Despite being significantly shorter (328-aa residues as compared with 502-508 aa in other AgI/II family proteins), the BspA-C domain exhibits a high degree of sequence identity to equivalent regions in other AgI/II family proteins, indicative of analogous function. The (8,9). This comprises a stalk consisting of the ␣-helical A domain and the polyproline II (PPII) helical P domain, separating the V domain and the C-terminal domains.…”

Section: Distribution Of Agi/ii Polypeptides In Gbs-mentioning

confidence: 99%

“…Bioinformatic analysis of the A and P domains from Bsp proteins demonstrates that these regions are significantly shorter than those of other AgI/II family polypeptides (117-168 residues for Bsp-A domains and 77-102 residues for Bsp-P domains) and differ considerably in amino acid composition. Most notably Bsp-A domains are largely devoid of the AXYXA(LV) heptad motif identified in SpaP and conserved in AspA and SspB (8). In an effort to reconcile these features, the A and P domains of BspA were produced recombinantly, and their ability to associate in vitro was examined.…”

Section: Bspa-a and -P Domains Form An Anti-parallel Coiled-coil Supementioning

confidence: 99%

“…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).…”

mentioning

confidence: 99%

“…The C-terminal region consists of a proline-rich repeat sequence (P) followed by a C-terminal domain (C) and an LPXTG motif required for bacterial cell wall anchorage. The A and P regions flank a central variable region (V), which exhibits the greatest strain-tostrain sequence variation between streptococci and is thought to confer ligand-binding specificity (8). Structural characterization of AgI/II family proteins from Streptococcus mutans (SpaP) and Streptococcus gordonii (SspB) has revealed a distinctive extended fibrillar structure that projects outwards from the wall-proximal C domain (Fig.…”

mentioning

confidence: 99%

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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: Discussionsupporting

confidence: 88%

Section: Distribution Of Agi/ii Polypeptides In Gbs-mentioning

confidence: 99%

Section: Bspa-a and -P Domains Form An Anti-parallel Coiled-coil Supementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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