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  • 1
    Electronic Resource
    Electronic Resource
    Eucaryotic cell components that bind to chlamydial elementary bodies: the histones (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 91 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract HeLa-cell-membrane fractions isolated by sonication as used previously to identify chlamydial adhesins were examined by a blotting technique for binding chlamydial elementary bodies (EB). One HeLa cell protein with apparent molecular mass of 32 kDa was found to bind native EB. A monoclonal antibody (mAb) raised against this chlamydial binding host-cell protein reacted with eucaryotic histones. Histone fractions were capable of binding EB in an ELISA assay and histone H1 was identified as the chlamydial-binding host cell protein in the Hela cell membrane fraction. Probing with specific mAbs against histone H3 and DNA confirmed that chromatin components were present in the host-cell membrane extract. These data suggest that the HeLa-cell-binding chlamydial proteins were previously identified by their reaction with chromatin and not with membrane components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05213.x
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  • 2
    Electronic Resource
    Electronic Resource
    Diagnosis of ovine enzootic abortion using an indirect ELISA (rOMP91B iELISA) based on a recombinant protein fragment of the polymorphic outer membrane protein POMP91B of Chlamydophila abortus (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 195 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Chlamydophila abortus is of major economic importance worldwide as one of the principal causes of abortion in sheep. Serological diagnosis of infection by the complement fixation test (CFT) is complicated by false positive reactions resulting from cross-reactive antibodies to Chlamydophila pecorum. To improve diagnosis an indirect enzyme-linked immunosorbent assay (iELISA) based on a recombinant protein fragment of the C. abortus polymorphic outer membrane protein POMP91B (rOMP91B iELISA) was assessed using a panel of 281 sera from experimentally and naturally infected sheep. The iELISA performed well, being more sensitive (84.2%) and specific (98.5%) than the CFT. Furthermore, the iELISA was better at differentiating C. abortus- from C. pecorum-infected animals. The new rOMP91B iELISA test will prove a valuable tool for the routine serodiagnosis of C. abortus infection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10514.x
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  • 3
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic localisation of the OMP90 family on the outer membrane surface of Chlamydia psittaci (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 164 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The putative outer membrane location of the OMP90 (formerly POMP) family from the ovine abortion strain of Chlamydia psittaci was investigated by immunoelectron microscopy. Using a non-embedding technique, antigens were shown to be localised on the outer membrane surface of both elementary and reticulate bodies, the infectious and non-infectious forms of Chlamydiae respectively. Antibodies affinity-purified against the expressed amino- and carboxy-terminal halves of one of the family members, OMP90A, demonstrated that the amino half is surface-exposed while the carboxyl half is most probably localised internally. Surface localisation on elementary bodies indicates the importance of these proteins as protective antigen candidates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13075.x
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  • 4
    Electronic Resource
    Electronic Resource
    Host passage-dependent wheat germ agglutinin-binding proteins of Chlamydia trachomatis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 81 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: Wheat germ agglutinin (WGA)-binding proteins in the highly purified elementary bodies (EB) of Chlamydia trachomatis were detected by an ELISA-like assay of immobilized EB. Trypsin-sensitivity of the WGA-binding moieties was detected only in the chlamydiae grown in HeLa cells. A nonionic detergent, β-octyl-D-glucopyranoside (OG), was used to extract proteins from the purified EB. Proteins in the extract were resolved by SDS-PAGE and probed with 125I-labelled WGA. Several proteins reacted with WGA in a specific manner. Some of these WGA-binding proteins in the EB of serovars L1 and E exhibited altered molecular mass after adaptation in the two alternate hosts, HeLa and McCoy cells. These results suggest that WGA-binding proteins exist in chlamydiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04711.x
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  • 5
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoretic analysis of the protein family at 90 kDa of abortifacient Chlamydia psittaci (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2104-2108 
    Details
    ISSN: 0173-0835
    Keywords: Abortifacient chlamydia ; 90 kDa antigens ; Envelope ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Four major clusters, designated A, B, C and D, were distinguished in Western Blots by a monoclonal antibody specific for the “antigen family at 90 kDa” after two-dimensional electrophoretic analysis on immobilized pH gradient of chlamydial elementary bodies of abortifacient C. psittaci. Clusters B, C, and D were closely related with molecular mass (kDa) pI values of 91.5/5.2-5.4, 90/5.0-5.2 and 90.5/5.6-5.8, respectively. Cluster A was larger, with molecular mass/pI of 104.7/5.1-5.3. Evidence for the antigenic relationship between cluster A and clusters B, C and D was further supported by immunological cross-reaction with affinity-purified antibodies from serum of ewes with chlamydial-induced abortion. The experimental values obtained for size and pI of the four clusters correlated well with the calculated values from known sequences coded by multiple chlamydial genes. Direct evidence for the correspondence between the immunoreactive clusters B, C and D and the retrieved genes was provided by antibody binding experiments to recombinant polypeptides representing fragments of the deduced proteins. The 4-member antigen family at 90/104 kDa is the first example of proteins coded by multiple genes within the genus Chlamydia.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181137
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  • 6
    Electronic Resource
    Electronic Resource
    Mapping of Chlamydia trachomatis proteins by Immobiline-polyacrylamide two-dimensional electrophoresis: Spot identification by N-terminal sequencing and immunoblotting (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 185-190 
    Details
    ISSN: 0173-0835
    Keywords: Chlamydia ; Two-dimensional polyacrylamide gel electrophoresis ; Protein maps ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins from purified elementary bodies of Chlamydia trachomatis were separated by two-dimensional gel electrophoresis on nonlinear wide-range immobilized pH gradients in the first dimension and polyacrylamide gradient gels in the second dimension. The maps obtained with this system are highly reproducible and resolve ca. 600 spots. By using immunoblot analysis with specific antibodies and/or N-terminal amino acid sequencing, we established the positions of a number of described chlamydial proteins, such as the major outer membrane protein (MOMP) the 60 kDa cystein-rich outer membrane protein (OMP2), the DnaK-like, GroEL-like, and macrophage infectivity potentiator (MIP)-like proteins, the plasmid-encoded pgp3 protein, two ribosomal proteins (S1 and L7/L12), and the protein-elongation factor EF-Tu. Other proteins, for which gene assignment was not possible, have been identified by three parameters (Mr, pI and N-terminal sequence). This work provides a preliminary basis for a future and progressive compilation of a genome-linked database of chlamydial proteins.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170130
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