Major Outer Membrane Proteins: Common Antigens in Enterobacteriaceae Species

Hofstra, H.; Dankert, J.

doi:10.1099/00221287-119-1-123

Cited by 45 publications

(41 citation statements)

References 28 publications

(26 reference statements)

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“…All the preparations were immunogenic in rabbits as determined by EIA. High antibody titres to the homologous antigens, but also rather high titres to heterologous antigens (porin, OmpA protein or lipoprotein) were observed, in keeping with the reported cross-reactions between enterobacterial OM proteins (Hofstra and Dankert, 1980). All the detected responses were of IgG class as expected for protein antigens.…”

Section: Discussionsupporting

confidence: 59%

“…The major outer-membrane (OM) proteins, including porins and the OmpA protein, show antigenic cross-reactivity within the family Enterobacteriaceae (Hofstra and Dankert, 1980), and this has raised the possibility of their use as vaccines (Kuusi et al, 1979). However, van der Ley et al (1986) have recently shown that anti-porin antibodies could not bind to their target antigen on smooth E. coli.…”

Section: Introductionmentioning

confidence: 99%

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Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model

Vuopio‐Varkila

Karvonen²,

Saxén³

1988

Journal of Medical Microbiology

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Section: Discussionsupporting

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model

Vuopio‐Varkila

Karvonen²,

Saxén³

1988

Journal of Medical Microbiology

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“…(1,15). In addition, EDTA and mild agitation has been shown to extract specifically outer membrane components from gram-negative bacteria including P. gingivalis (9,12). Coupled with the finding that the extraction procedure did not cause noticeable cell disruption, as determined by Gram staining and by measuring viable counts, it is reasonable to conclude that the biotinylated molecules in this preparation are surface exposed.…”

Section: Methodsmentioning

confidence: 91%

Identification of a Porphyromonas gingivalis Receptor for the Streptococcus gordonii SspB Protein

2000

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Colonization of the plaque biofilm by the oral pathogen Porphyromonas gingivalis is favored by the presence of antecedent organisms such as Streptococcus gordonii. Coadhesion between P. gingivalis and S. gordonii can be mediated by the SspB protein of S. gordonii; however, the P. gingivalis cognate receptor for this protein has not been identified. In this study, we identified a surface protein of P. gingivalis that interacts with the SspB protein. Coprecipitation between P. gingivalis outer membrane proteins and purified SspB protein demonstrated that a 100-kDa P. gingivalis protein bound to SspB. The 100-kDa protein also bound to an engineered strain of Enterococcus faecalis that expresses the SspB protein on the cell surface. Monospecific polyclonal antibodies to the 100-kDa protein inhibited the binding between P. gingivalis and S. gordonii in a dose-dependent manner up to 86%. Amino acid sequencing of the 100-kDa protein showed homology to a protein previously identified as the P. gingivalis minor fimbria. The minor fimbrial protein may exist as a complex with a hemagglutinin-like protein since the genes encoding these proteins are adjacent on the chromosome and are cotranscribed. Thus, the P. gingivalis receptor for S. gordonii SspB is a 100-kDa protein that structurally may be a minor fimbriaprotein complex and functionally effectuates coadhesion.Porphyromonas gingivalis, a gram-negative anaerobic coccobacillus, is an etiologic agent of severe adult periodontitis, a chronic inflammatory disease that can cause destruction of periodontal tissues and resorption of the alveolar bone, with eventual exfoliation of teeth (17, 21). Colonization of the oral cavity by P. gingivalis is facilitated by adherence to various oral surfaces, including epithelial cells, the salivary pellicle that coats tooth surfaces, and other oral bacteria that comprise the plaque biofilm. P. gingivalis is a secondary colonizer of plaque, adhering to the primary colonizers including Actinomyces species and oral streptococci such as Streptococcus gordonii (11,20,22). In vivo studies have demonstrated that P. gingivalis preferentially colonizes preformed early plaque over other oral sites, suggesting that the interaction between the early colonizers and P. gingivalis is important in the development of pathogenic plaque (20). In vitro, P. gingivalis adheres avidly to sessile S. gordonii and, once attached, rapidly forms a biofilm comprising towering microcolonies separated by fluid-filled channels (3).Adhesion between P. gingivalis and S. gordonii is multimodal, involving a number of distinct adhesin-receptor pairs on the surfaces of both organisms. These molecules include the major fimbriae and a 35-kDa protein of P. gingivalis and the Ssp proteins of S. gordonii (10, 12). The Ssp proteins are members of the antigen I/II family of major streptococcal surface proteins and are multifunctional adhesins (2). In S. gordonii, tandem genes encode the SspA and SspB polypeptides, which are highly similar with respect to structure and function (6). ...

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“…This antiserum was obtained from the same rabbit that had earlier been used to prepare the OmpF-specific antiserum. However the rabbit had in the meantime been reinoculated with OmpF protein (the same preparation originally used), and it is therefore probable that this batch of OmpF protein was contaminated by a small amount of OmpA protein (not detected on gels due to the intense OmpF protein band), as has been reported for other purified OmpF preparations [9]. The original OmpF-specific antiserum also precipitated a small amount of OmpA protein, an observation which we earlier suggested might have been due to 'non-specific' precipitation [5].…”

Section: Antiserumentioning

confidence: 98%

Rate of Translation and Kinetics of Processing of Newly Synthesized Molecules of Two Major Outer‐Membrane Proteins, the OmpA and OmpF Proteins, of Escherichia coli K12

Crowlesmith¹,

Gamon²

1982

European Journal of Biochemistry

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The rate of synthesis of the OmpA and OmpF proteins, two of the major outer membrane proteins of E.sckerichia coli K12, was determined. At 25 "C both proteins were translated at 6.5 amino acids/s, and the OmpF protein was translated at 15 amino acids/s at 37 "C. The former rate corresponded to a synthesis time of just over SO s for both proteins, which is significantly faster than their reported rates of assembly into the outer membrane at 25 "C. The kinetics of processing of the pro-OmpF protein were also investigated in detail, and the pro-OmpF half-life estimated to be 3 -5 s at 25 "C. However a fraction of the precursor was processed more slowly, which may explain the discrepancy between these data and our earlier published estimate of 30 s. Pro-OnipA protein was processed with similar kinetics. These results demonstrate that the rate-limiting step in the assembly of both proteins into the outer membrane is post-translational and follows the processing step.The outer membrane proteins of gram-negative bacteria share a number of biosynthetic steps with two other classes of exported protein, the inner membrane and periplasmic proteins. These include: translation, export (i.e. transfer across the inner membrane) and processing (for proteins synthesized initially in precursor form). In addition, outer membrane proteins must be translocated to the outer membrane. Despite these similarities the rate of assembly of outer membrane proteins is two or three times slower than that of inner membrane proteins (though perhaps faster than that of periplasmic proteins) at 25-30 "C [I -41. Intuitively it would seem that the rate-limiting step in outer membrane protein assembly must be either translocation (the only step unique to outer membrane proteins) or processing (which should not affect the kinetics of inner membrane protein assembly). In an earlier paper [ S ] we reported that newly synthesized pro-OmpF protein had a relatively long half-life of 30 s, suggesting that the processing reaction might be ratelimiting for assembly. However, we also found that newly synthesized, processed molecules of both OmpF and OmpA proteins were present in the inner membrane after a 10-s pulse ; these results suggest that translocation may be rate-These results are at odds with those of Lin and Wu [2], who have suggested that the rate-limiting step in outer membrane protein assembly is translation of the niRNA. However, their evidence is indirect and not in accordance with the data of Boyd and Holland [6], who could detect no difference between the 'run-out' times (a crude measure of the translation rate) of the OmpF protein and a representative cytoplasmic protein in Escherichia coli Bjr.In view of these problems we decided to reinvestigate the kinetics of processing of the OmpF and OmpA proteins and to measure directly their rates of synthesis. Our results indicate that neither processing nor translation are slow enough to permit them to be considered rate-limiting. Since the only steps to follow processing are translocation and irre...

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Major Outer Membrane Proteins: Common Antigens in Enterobacteriaceae Species

Cited by 45 publications

References 28 publications

Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model

Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model

Identification of a Porphyromonas gingivalis Receptor for the Streptococcus gordonii SspB Protein

Rate of Translation and Kinetics of Processing of Newly Synthesized Molecules of Two Major Outer‐Membrane Proteins, the OmpA and OmpF Proteins, of Escherichia coli K12

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