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  • 1
    Electronic Resource
    Electronic Resource
    Molecular cloning of the S-layer protein gene of Campylobacter rectus ATCC 33238 (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A genomic DNA library of Campylobacter rectus (Wolinella recta) ATCC 33238 was constructed using bacteriophage lambda EMBL3 as a vector. One clone expressing the S-layer protein was identified immunologically with the antiserum to the S-layer protein of C. rectus ATCC 33238. Western immunoblotting using monoclonal antibodies directed against the S-layer protein showed a single blot of recombinant protein at 150 kDa, suggesting that this clone contained the entire coding region of the S-layer protein gene. Additionally, the S-layer protein gene was subcloned into plasmid vector pUC18. Southern hybridization revealed that the S-layer protein gene was present on the chromosome of C. rectus as a single-copy gene, and that there were minor heterogeneities among the S-layer protein genes of clinical isolates. Moreover, a spontaneous stable mutant strain, which has no S-layer expression, also conserved the full-length gene of the S-layer protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06668.x
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  • 2
    Electronic Resource
    Electronic Resource
    Colonial variation and fimbriation of Actinobacillus actinomycetemcomitans (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 69 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Three colonial variants of Actinobacillus actinomycetemcomitans, which formed transparent rough (TR)-, transparent smooth (TS)-, and opaque smooth (OS)-surfaced colonies, were described in relation to their fimbriation. TR- and TS-cells were adhesive to agar and glass surfaces but not the OS-cells. The examination by electron microscopy revealed that TR-cells were highly fimbriated but not TS- and OS-cells. Thus, TS-cells seemed to be an intermediate type. The fimbriae were isolated from TR-cells by suspending in 0.15 M ethanolamine-HCl buffer (pH 10.5) and purified by dissolving non-fimbrial components in 0.5% deoxycholate and 0.7% n-octyl-β-d-glucopyranoside. The relative molecular mass of the fimbrial subunit protein was 54 000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb04167.x
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  • 3
    Electronic Resource
    Electronic Resource
    Antigenic properties of Campylobacter rectus (Wolinella recta) major S-layer proteins (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 108 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The antigenic properties of the surface layer (S-layer) proteins of various Campylobacter rectus strains including 24 clinical isolates and the type strain ATCC 33238 were examined. S-layer proteins were extracted from whole cells by acid treatment according to the method of McCoy et al. (Infect. Immun. 11, 517–525, 1975). The acid extracts from 23 of the isolates and ATCC 33238 contained two major proteins with molecular masses of 130 kDa and 150 kDa, both of which were identified as subunits of the S-layer after comparison with the protein profiles of acid-treated (S-layer-deficient) cells. An S-layer protein from one isolate (CI-808) demonstrated a different molecular mass (160 kDa). Both the 150-kDa proteins of ATCC 33238 and isolate CI-306 and the 160-kDa protein of CI-808 were purified by ion-exchange chromatography in the presence of urea. In Ouchterlony immunodiffusion experiments with these purified proteins and rabbit antiserum raised to each purified protein, both common and strain-specific antigenic determinants were identified in the C. rectus S-layer proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06115.x
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