The group B streptococcal alpha C protein binds α 1 β 1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells

Bolduc, Gilles R.; Madoff, Lawrence C.

doi:10.1099/mic.0.2007/009134-0

Cited by 29 publications

(29 citation statements)

References 60 publications

(62 reference statements)

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“…Consequently, mutations that alter glycosaminoglycan binding render GBS deficient in cervical epithelial cell invasion [165]. Furthermore, ACP can also promote GBS invasion of these host cells by binding to α 1 β 1 -integrins on the epithelial cell surface [166]. The mechanisms involved in the regulation of ACP expression are not understood.…”

Section: Adherence and Invasion Of Host-cell Surfacesmentioning

confidence: 99%

Understanding the Regulation of Group B Streptococcal Virulence Factors

2009

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Bacterial infections remain a significant threat to the health of newborns and adults. Group B Streptococci (GBS) are Gram-positive bacteria that are common asymptomatic colonizers of healthy adults. However, this opportunistic organism can also subvert suboptimal host defenses to cause severe invasive disease and tissue damage. The increasing emergence of antibiotic-resistant GBS raises more concerns for sustained measures in treatment of the disease. A number of factors that are important for virulence of GBS have been identified. This review summarizes the functions of some well-characterized virulence factors, with an emphasis on how GBS regulates their expression. Regulatory and signaling molecules are attractive drug targets in the treatment of bacterial infections. Consequently, understanding signaling responses of GBS is essential for elucidation of pathogenesis of GBS infection and for the identification of novel therapeutic agents.

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Section: Adherence and Invasion Of Host-cell Surfacesmentioning

confidence: 99%

Understanding the Regulation of Group B Streptococcal Virulence Factors

2009

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“…In a second possible mechanism, one of two N-terminal ACP domains promotes GBS invasion by binding α1β1-integrins on the epithelial cell surface (Ref. 33). …”

Section: Invasion Across Host Epithelial Barriersmentioning

confidence: 99%

Recent advances in understanding the molecular basis of group BStreptococcusvirulence

Maisey

Doran

Nizet

2008

Expert Rev. Mol. Med.

174

140

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Group B Streptococcus commonly colonises healthy adults without symptoms, yet under certain circumstances displays the ability to invade host tissues, evade immune detection and cause serious invasive disease. Consequently, Group B Streptococcus remains a leading cause of neonatal pneumonia, sepsis and meningitis. Here we review recent information on the bacterial factors and mechanisms that direct host-pathogen interactions involved in the pathogenesis of Group B Streptococcus infection. New research on host signalling and inflammatory responses to Group B Streptococcus infection is summarised. An understanding of the complex interplay between Group B Streptococcus and host provides valuable insight into pathogen evolution and highlights molecular targets for therapeutic intervention.GBS (Group B Streptococcus/-cocci) is a leading agent of severe, invasive bacterial infection in human newborns. Neonatal infection with this opportunistic pathogen can present as earlyonset or late-onset disease. In early-onset cases, bacteria are transferred from the mother to the infant in utero, following ascending infection of the placental membranes, or during passage through the birth canal, by aspiration of infected vaginal fluids. Early-onset neonatal infection manifests within the first few hours or days of life, often presenting as pneumonia and respiratory failure, which can quickly progress to bacteraemia and septic shock. By contrast, late-onset GBS disease can occur in infants up to several months old, and is distinguished by bloodstream infection with a high rate (40-60%) of progression to meningitis (Ref. 1). Infants that survive GBS meningitis can suffer serious long-term neurological consequences, such as seizures, hearing loss and cognitive impairment. Serious GBS infections are increasingly recognised in adult populations, particularly in the elderly and individuals compromised by underlying medical conditions. More than 40% of all invasive GBS cases in the USA occur past infancy (Ref. 2).The development of GBS disease reflects successful bacterial colonisation of the vaginal epithelium, penetration of placental or epithelial barriers, resistance to immune clearance allowing bloodstream survival and, in cases of meningitis, the ability to breach the endothelial blood-brain barrier (BBB). In overcoming these obstacles, GBS expresses a diverse array of surface-associated and secreted virulence factors that mediate specific host-cell interactions and interfere with innate immune clearance mechanisms. The present review explores

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“…Binding of GAS to epithelial cells involves an interaction between M protein and fibronectin (Oehmcke et al, 2010). Epithelial cell invasion by Group B Streptococcus (GBS) is associated with expression of alpha C protein (Bolduc and Madoff, 2007). Aggregation protein encoded by asp1 gene of enterococci, characterized as a virulence factor of 142 kDa plays a crucial role in adherence to eukaryotic cells (Galli et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Shortening of the Lactobacillus paracasei subsp. paracasei BGNJ1-64 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation

et al. 2016

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AggLb is the largest (318.6 kDa) aggregation-promoting protein of Lactobacillus paracasei subsp. paracasei BGNJ1-64 responsible for forming large cell aggregates, which causes auto-aggregation, collagen binding and pathogen exclusion in vitro. It contains an N-terminus leader peptide, followed by six successive collagen binding domains, 20 successive repeats (CnaB-like domains) and an LPXTG sorting signal at the C-terminus for cell wall anchoring. Experimental information about the roles of the domains of AggLb is currently unknown. To define the domain that confers cell aggregation and the key domains for interactions of specific affinity between AggLb and components of the extracellular matrix, we constructed a series of variants of the aggLb gene and expressed them in Lactococcus lactis subsp. lactis BGKP1-20 using a lactococcal promoter. All of the variants contained a leader peptide, an inter collagen binding-CnaB domain region (used to raise an anti-AggLb antibody), an anchor domain and a different number of collagen binding and CnaB-like domains. The role of the collagen binding repeats of the N-terminus in auto-aggregation and binding to collagen and fibronectin was confirmed. Deletion of the collagen binding repeats II, III, and IV resulted in a loss of the strong auto-aggregation, collagen and fibronectin binding abilities whereas the biofilm formation capability was increased. The strong auto-aggregation, collagen and fibronectin binding abilities of AggLb were negatively correlated to biofilm formation.

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The group B streptococcal alpha C protein binds α 1 β 1-integrin through a novel KTD motif that promotes internalization of GBS within human epithelial cells

Cited by 29 publications

References 60 publications

Understanding the Regulation of Group B Streptococcal Virulence Factors

Understanding the Regulation of Group B Streptococcal Virulence Factors

Recent advances in understanding the molecular basis of group BStreptococcusvirulence

Shortening of the Lactobacillus paracasei subsp. paracasei BGNJ1-64 AggLb Protein Switches Its Activity from Auto-aggregation to Biofilm Formation

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