1887

Abstract

N-terminal sequence analysis of peptides generated by proteolytic treatment of the OE 28.3 major outer-membrane protein OprF, embedded in outer membranes or present in whole cells, indicated a surface-exposed location for the proline-rich region of the protein. This region is absent from the and OprFs. Evidence was obtained for the presence of additional exposed but less accessible regions in the carboxy half of OprF. Four OprF-specific monoclonal antibodies were all directed to the C-terminal part of the protein but did not recognize a surface-exposed epitope as shown by flow cytometry. Our data support the model previously proposed for OprF in which the entire protein is embedded in the outer membrane, unlike the topology proposed for the major outer-membrane protein from , OmpA, whose carboxy half resides in the periplasmic space. For six other strains producing OprF proteins with different isoelectric points, the primary structure was determined by sequence analysis of the PCR-amplified genes. The proline-rich domain represented the most conserved region of the different OprFs. Based on the sequence of its gene, it was shown that the mushroom pathogen is quite closely related to . Comparative sequence analysis further showed that the carboxy half of OprF contains a sequence motif that is well conserved in the enterobacterial OmpA proteins but is also present in a number of other outer-membrane proteins, including peptidoglycan-associated lipoproteins.

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/content/journal/micro/10.1099/00221287-140-6-1377
1994-06-01
2019-10-23
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-6-1377
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