Molecular cloning, nucleotide sequence, and occurrence of a 16.5-kilodalton outer membrane protein of Brucella abortus with similarity to pal lipoproteins

Tibor, Anne; Weynants, Vincent; Denoël, Philippe; Lichtfouse, Bernadette; Bolle, Xavier De; Saman, Eric; Limet, J N; Letesson, Jean‐Jacques

doi:10.1128/iai.62.9.3633-3639.1994

Cited by 61 publications

(51 citation statements)

References 45 publications

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“…This study was undertaken to explore the role of the tolQ and tolR genes in E. ictaluri virulence. The organization of the tol operon in the E. ictaluri chromosome is similar to the tol operon in other Gram-negative pathogens, including Pseudomonas putida [21], Actinobacillus actinomycetemcomitans [22], Erwinia chrysanthemi [23], Brucella abortus [24], and Haemophilus influenza [25,26]. As expected, there is high amino acid identity between Tol system proteins encoded by E. ictaluri, E. tarda, and E. coli.…”

Section: Discussionsupporting

confidence: 67%

Involvement of tolQ and tolR genes in Edwardsiella ictaluri virulence

Abdelhamed

Lawrence

et al. 2016

Microbial Pathogenesis

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Edwardsiella ictaluri is a Gram-negative intracellular facultative pathogen causing enteric septicemia of channel catfish (ESC). The Tol system, consisting of four envelope proteins TolQ, TolR, TolA, and TolB, are required for colicin import and contributes to bacterial virulence in several pathogenic bacteria. However, the Tol system and its importance in E. ictaluri virulence have not been investigated. Here we present construction and evaluation of the E. ictaluri TolQ, TolR and TolQR mutants (EiΔtolQ, EiΔtolR, and EiΔtolQR). The Tol mutants were developed using in-frame gene deletion and their attenuation and vaccine efficacy were determined in catfish fingerlings. The EiΔtolQ, EiΔtolR, and EiΔtolQR mutants showed reduced virulence in catfish (28.93%, 19.70%, and 39.82% mortality, respectively) compared to wild type (46.91% mortality). Further, vaccination with these mutants protected catfish against subsequent wild-type infection. This study suggests that the Tol system contributes to E. ictaluri virulence in catfish.

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Section: Discussionsupporting

confidence: 67%

Involvement of tolQ and tolR genes in Edwardsiella ictaluri virulence

Abdelhamed

Lawrence

et al. 2016

Microbial Pathogenesis

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“…A serologically reactive minor OMP (OMP16.5) was also present in the 17-kDa region. This protein is distinct from the 17-kDa antigen described here, as shown by its reactivity toward specific MAbs (2) as well as by its primary sequence (18). The serological prevalence of the 17-kDa antigen was also studied with a MAb in a competition ELISA.…”

Section: Discussionmentioning

confidence: 92%

Cloning and sequence analysis of a newly identified Brucella abortus gene and serological evaluation of the 17-kilodalton antigen that it encodes

Hemmen

Weynants

Scarcez

et al. 1995

Clin Diagn Lab Immunol

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A thus far unknown gene encoding a Brucella abortus protein has been isolated from a lambda gt11 expression library probed with sera from Brucella-infected sheep. Sequence analysis of the cloned gene revealed the presence of an open reading frame of 158 amino acids encoding a protein of 17.3 kDa (calculated molecular mass). The recombinant B. abortus protein, expressed in Escherichia coli, and the corresponding Brucella melitensis protein migrated at the same apparent molecular masses as shown by Western blotting (immunoblotting). Among a series of serum samples from B. melitensis-or B. abortus-infected sheep and cows, 51 and 39%, respectively, showed a signal at 17 kDa on Western blot analysis of total protein extract from Brucella bacteria. These figures amount to 70 and 61% for sheep and cattle, respectively, in a competitive enzyme-linked immunosorbent assay with a specific monoclonal antibody. These data indicate that the 17-kDa antigen may be useful for serological diagnosis of Brucella infection.

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“…The C-terminal region of CadF also possesses an alpha-helical consensus motif (NX 2 LSX 2 RAX 2 VX 3 l), which is proposed to be involved in the non-covalent association of Omps with peptidoglycan (Koebnik, 1995). This consensus motif has previously been identified in a number of proteins, including Omp18 from C. jejuni , PAL of E. coli (Chen and Henning, 1987;Lazzaroni and Portalier, 1992), Omp16 from Brucella abortus (Tibor et al, 1994), P6 of Haemophilus influenzae (Deich et al, 1988;Nelson et al, 1988), PplA of Legionella pneumophila (Engleberg et al, 1991;Ludwig et al, 1991), and OmpA from Enterobacteriaceae. Finally, searches using the deduced amino acid sequence of CadF revealed greatest similarity to the Omp porin F (OprF) from Pseudomonas species, including P. fluorescens and Pseudomonas tolaasi (De Mot et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

Konkel

Garvis

Tipton

et al. 1997

Molecular Microbiology

288

238

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SummaryCampylobacter jejuni, a Gram-negative bacterium, is a common cause of gastrointestinal disease. By analogy with other enteric pathogens such as Salmonella and Shigella, the ability of C. jejuni to bind to host cells is thought to be essential in the pathogenesis of enteritis. Scanning electron microscopy of infected INT407 cells suggested that C. jejuni bound to a component of the extracellular matrix. Binding assays using immobilized extracellular matrix proteins and soluble fibronectin showed specific and saturable binding of fibronectin to C. jejuni. Ligand immunoblot assays using 125 I-labelled fibronectin revealed specific binding to an outer membrane protein with an apparent molecular mass of 37 kDa. A rabbit antiserum, raised against the gel-purified protein, reacted with a 37 kDa protein in all C. jejuni isolates (n ¼ 15) as tested by immunoblot analysis. Antibodies present in convalescent serum from C. jejuni-infected individuals also recognized a 37 kDa protein. The gene encoding the immunoreactive 37 kDa protein was cloned and sequenced. Sequencing of overlapping DNA fragments revealed an open reading frame (ORF) that encodes a protein of 326 amino acids with a calculated molecular mass of 36 872 Da. The deduced amino acid sequence of the ORF exhibited 52% similarity and 28% identity to the root adhesin protein from Pseudomonas fluorescens. Isogenic C. jejuni mutants which lack the 37 kDa outer membrane protein, which we have termed CadF, displayed significantly reduced binding to fibronectin. Biotinylated fibronectin bound to a protein with an apparent molecular mass of 37 kDa in the outer membrane protein extracts from wild-type C. jejuni as judged by ligandbinding blots. These results indicate that the binding of C. jejuni to fibronectin is mediated by the 37 kDa outer membrane protein which is conserved among C. jejuni isolates.

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Molecular cloning, nucleotide sequence, and occurrence of a 16.5-kilodalton outer membrane protein of Brucella abortus with similarity to pal lipoproteins

Cited by 61 publications

References 45 publications

Involvement of tolQ and tolR genes in Edwardsiella ictaluri virulence

Involvement of tolQ and tolR genes in Edwardsiella ictaluri virulence

Cloning and sequence analysis of a newly identified Brucella abortus gene and serological evaluation of the 17-kilodalton antigen that it encodes

Identification and molecular cloning of a gene encoding a fibronectin‐binding protein (CadF) from Campylobacter jejuni

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