Multiple mouse-protective antibodies directed against group B streptococci. Special reference to antibodies effective against protein antigens.

Lancefield, Rebecca C.; McCarty, Maclyn; Everly, W N

doi:10.1084/jem.142.1.165

Cited by 345 publications

(163 citation statements)

References 11 publications

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“…S. agalactiae is a B group Streptococcus that causes meningitis in newborns (Jerlstrom et al, 1991). The IgA Fc receptor is part of the c complex that may contribute to the virulence of this organism (Lancefield et al, 1975). Two specific IgA-binding regions have been defined; the second of these two regions contains the Ig-like domain (Jerlstrom et al, 1991).…”

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confidence: 99%

Members of the immunoglobulin superfamily in bacteria

1996

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Abstract:We report a prediction that two prokaryotic proteins contain immunoglobulin superfamily domains. Immunoglobulinlike folds have been identified previously in prokaryotic proteins, but these share no recognizable sequence similarity with eukaryotic immunoglobulin superfamily (IgSF) folds, and may be the result of the physics and chemistry of proteins favoring certain common folds. In contrast, the prokaryotic proteins identified have sequences whose match to the immunoglobulin superfamily can be detected by hidden Markov modeling, BLASTP matches, key residue analysis, and secondary structure predictions. We propose that these prokaryotic immunoglobulin-like domains are almost certain to be related by divergence from a common ancestor to eukaryotic immunoglobulin superfamily domains.

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confidence: 99%

Members of the immunoglobulin superfamily in bacteria

1996

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“…In this vertical immunization model, cross protection between types Ia and Ia/c was shown at low levels only in the neonates delivered from type Ia/c-immunized mothers. Antibody to Iabc carbohydrate antigen, which we did not estimate, was reported to be protective (20), but less potent than the Ia antibody. Another interpretation is that the type Ia organisms are more sensitive to opsonization in the presence of Ia or Iabc antibody (14).…”

Section: Discussionmentioning

confidence: 90%

Protective Efficacy against Group B Streptococcal Infection in Neonatal Mice Delivered from Preimmunized Pregnants

Itoh¹,

Yan²,

Nakano³

et al. 1986

Microbiology and Immunology

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Neonatal mice delivered from mothers preimmunized with heated or formalinized whole cell vaccines of type Ia, Ia/c and III/c group B streptococci were infected with each type of bacteria, and then serum antibodies of mothers and neonates who survived the experiments were measured by enzyme-linked immunosorbent assay. The relationship between the protectivity in neonate mice and the antibody titers to the type specific polysaccharide antigens and the protein c antigen of their sera were examined.In the Ia-immunized group which showed high protection against the type Ia infection, anti-Ia IgG antibody titers were low, and anti-protein c IgG antibody was riot detected. Type Ia/c and Mk vaccines were highly effective against both type Ia/c and III/c infection, but less effective in type Ia infection. The protein c antigen was identified in both type strains by the double diffusion assay, and the IgG antibodies to the protein c were significantly high in sera of both maternal mice immunized with types Ia/c or III/c organisms and their newborn infants. High titers of the protein c IgG antibody retained 3 to 4 weeks after the last injection of vaccines which corresponded to the period of pregnancy and lactation. Small amounts of IgM antibody to all antigens were detected only in maternal sera.These results suggest that IgG antibodies to the protein c antigen and to the type-specific polysaccharide antigens are equally important protective factors which are transferable from preimmunized mothers to their newborn infants through placenta and/or lactation.Group B streptococcus is recognized as an important agent of sepsis and meningitis in neonates, and is transmitted to newborn infants in the maternal genital tracts (2, 12, 13). Group B streptococci (GBS) are known to be colonized in the vaginas of, at most, 70% of all pregnant women (1), but only about 1% of their newborns seem to develop serious GBS diseases (18). The low rate of apparent infection could be derived from defence mechanisms in the neonates. Baker and her colleagues (3)(4)(5) found that the susceptibility of neonates to infection with type III GBS is related to the absence of transmitted maternal immunoglobulin G (IgG) antibody to type III polysaccharide, which has been corroborated by others 297

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“…GBS type Ia/C (a+, b+) strain A909 and the ACP-deficient mutant JL2053 have been described (Li et al, 1997). A909 was obtained from Dr Rebecca Lancefield (Lancefield et al, 1975). JL2053 was obtained from Dr Jing Li.…”

Section: Methodsmentioning

confidence: 99%

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

Madoff

2007

Microbiology

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Group B Streptococcus (GBS) is the leading cause of bacterial pneumonia, sepsis and meningitis among neonates and a cause of morbidity among pregnant women and immunocompromised adults. GBS epithelial cell invasion is associated with expression of alpha C protein (ACP). Loss of ACP expression results in a decrease in GBS internalization and translocation across human cervical epithelial cells (ME180). Soluble ACP and its 170 amino acid N-terminal region (NtACP), but not the repeat protein RR9, bind to ME180 cells and reduce internalization of wild-type GBS to levels obtained with an ACP-deficient isogenic mutant. In the current study, ACP colocalized with a 1 b 1 -integrin, resulting in integrin clustering as determined by laser scanning confocal microscopy. NtACP contains two structural domains, D1 and D2. D1 is structurally similar to fibronectin's integrin-binding region (FnIII10). D1's (KT)D146 motif is structurally similar to the FnIII10 (RG)D1495 integrin-binding motif, suggesting that ACP binds a 1 b 1 -integrin via the D1 domain. The (KT)D146A mutation within soluble NtACP reduced its ability to bind a 1 b 1 -integrin and inhibit GBS internalization within ME180 cells. Thus ACP binding to human epithelial cell integrins appears to contribute to GBS internalization within epithelial cells. INTRODUCTIONGroup B Streptococcus (GBS; Streptococcus agalactiae) is the leading cause of neonatal bacterial invasive diseases (Arisoy et al., 2003;Manning et al., 2004). The organism colonizes the vagina, rectum and urethra of 10-35 % of adults without causing disease. Neonates acquire GBS either in utero or during birth, aspirating GBS-containing fluid. GBS enters the lungs, binds to and invades the alveolar epithelial cells, and enters the blood, allowing the organisms to infect multiple organs. Invasive disease occurs within hours of birth, with 4-6 % mortality (Baker & Edwards, 1995;Schrag et al., 2000). In a survey in the USA, the incidence of early-onset disease (within the first week of life) declined by 65 % (from 1.7 per 1000 live births to 0.6 per 1000) from 1993 to 1998, due to intrapartum antimicrobial prophylaxis (Schrag et al., 2000) and stabilized at 0.35 per 1000 in 2004 . The incidence of late-onset disease (.1 week to 3 months of age) remained stable, with an average of 0.35 per 1000 live births during the same time period (CDC, 1997(CDC, , 2005.GBS was more recently found to be pathogenic in the elderly, and in adults with underlying medical conditions, including diabetes (Dahl et al., 2003;Jackson et al., 1995;Tyrrell et al., 2000). Adult invasive GBS diseases result in bacteraemia, meningitis, skin and soft-tissue infection, and bone and joint infections. The rate of invasive diseases is significantly higher in neonates than in adults. However, the case fatality rates are greater in adults (Schuchat, 1999), with the incidence of GBS disease increasing with advanced age (Farley et al., 1993). Despite the clinical importance of these diseases, little is known about the events that lead up to GBS inv...

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Multiple mouse-protective antibodies directed against group B streptococci. Special reference to antibodies effective against protein antigens.

Cited by 345 publications

References 11 publications

Members of the immunoglobulin superfamily in bacteria

Members of the immunoglobulin superfamily in bacteria

Protective Efficacy against Group B Streptococcal Infection in Neonatal Mice Delivered from Preimmunized Pregnants

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

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