Paenibacillus larvae subsp. larvae (P. l. larvae) is the aetiological agent of American foulbrood (AFB), the most virulent bacterial disease of honey bee brood worldwide. In many countries AFB is a notifiable disease since it is highly contagious, in most cases incurable and able to kill affected colonies. Genotyping of field isolates of P. l. larvae revealed at least four genotypes (AB, Ab, ab and aB) present in Germany which are genotypically different from the reference strain DSM 7030. Therefore, based on these data, five different genotypes of P. l. larvae are now identified with genotype AB standing out with a characteristic brown-orange and circled two-coloured colony morphology. Analysing the metabolic profiles of three German genotypes (AB, Ab and ab) as well as of the reference strain using the Biolog system, a characteristic biochemical fingerprint could be obtained for each strain. Cluster analysis showed that while genotypes Ab, ab and the reference strain DSM 7030 are rather similar, genotype AB is clearly different from the others. Analysis of all isolates for plasmid DNA revealed two different plasmids present only in isolates belonging to genotype AB. Therefore, genotype AB is remarkable in all aspects analysed so far. Future analysis will show whether or not these differences will expand to differences in virulence.
Ha n nover, B isc hof s hole r Damm 15,30173 Hannover, Germany Microbiology, Surface antigenic variation was investigated in Mycop/asma arthritidis, an agent that produces chronic arthritis in rats which shares several features with many mycoplasma-induced diseases and thus defines a well-characterized model system. Hyperimmune rabbit antisera (anti-ISRI, anti-PG6, anti-H606 and anti-158~10) to whole M. arthritidis organisms were used as immunological probes in Western immunoblots of four M. arthritidis prototype strains (ISRI, PG6, H606 and D263) and five rat-passaged substrains (ISRlpl, ISRlp7, ISRlp8, 1 5 8 ~ 1 0 and D263pl). Several prominent antigens were identified that varied in expression. By Triton X-114 phase fractionation and treatment of whole cells with trypsin and carboxypeptidase Y, these strain-variant antigens were shown to be integral membrane proteins with C-termini and portions of the polypeptide chains oriented outside the membrane. Western blot immunoscreening of a large number of randomly selected clonal isolates and well-established clonal lineages from stock cultures of M. arthritidis ISRlp7, 158~10, PG6 and H606 revealed an expanded repertoire of variant membrane proteins whose expression was subject to independent, reversible phase variation. Colony immunoblots of these clonal populations with a hyperimmune rabbit antiserum to a gel-purif ied variant membrane protein (P36) showed that this phase switching occurred at a high frequency lo-* per generation). Detailed immunological and biochemical characterization of the phase-variant membrane proteins demonstrated that they are: (i) antigenically related or distinct; (ii) apparently specific to particular strain populations; (iii) proteins or lipoproteins; (iv) major immunogens of M. arthritidis, recognized by serum antibodies from convalescent rat; and (v) able to undergo variation in expression during in viwo passage. Thus, M. arthritidis possesses a complex system capable of creating large repertoires of cell surface phenotypes which may affect the multiple interactions of this organism with its host and dictate its potential as a successful infectious agent and pathogen. to
The electrophoretical separations of Mycoplasma arthritidis and the serum used in the cultivation medium show a high number of protein bands with identical molecular weights. Proteins with molecular weights of 84, 72 and 52 kDa also appeared to be identical with proteins of Mycoplasma arthritidis in their antigenic properties as demonstrated by Western blotting with rat-anti-Mycoplasma arthritidis serum. The autoradiography of electrophoretically separated Mycoplasma arthritidis cells metabolically labeled with 35S-methionine and 35S-cysteine revealed that the proteins of Mycoplasma arthiritidis identical in molecular weight and antigenic structure with serum proteins are synthesized by Mycoplasma arthritidis, and represent true translation products.
The electrophoretical separations of Mycoplasma arthritidis and the serum used in the cultivation medium show a high number of protein bands with identical molecular weights. Proteins with molecular weights of 84, 72 and 52 kDa also appeared to be identical with proteins of Mycoplasma arthritidis in their antigenic properties as demonstrated by Western blotting with rat-anti-Mycoplasma arthritidis serum. The autoradiography of electrophoretically separated Mycoplasma arthritidis cells metabolically labeled with 35S-methionine and 35S-cysteine revealed that the proteins of Mycoplasma arthiritidis identical in molecular weight and antigenic structure with serum proteins are synthesized by Mycoplasma arthritidis, and represent true translation products.
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