Structural and functional properties of the p60 proteins from different Listeria species

The major extracellular protein p60 of Listeria monocytogenes seems to be required for this microorganism's adherence to and invasion of 3T6 mouse fibroblasts but not for adherence to human epithelial Caco-2 cells. Western blot analysis with polyclonal antibodies against p60 of L. monocytogenes...

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Bibliographic Details
Published in:Journal of Bacteriology 1992-12, Vol.174 (24), p.8166-8171
Main Authors: Bubert, A. (Universitat Wurzburg, Wurzburg, Germany), Kuhn, M, Goebel, W, Kohler, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacteria
Bacterial Adhesion
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Base Sequence
Biological and medical sciences
cell adhesion
Cell Line
DNA, Single-Stranded
ESPECE
ESPECIES
Fundamental and applied biological sciences. Psychology
Humans
LISTERIA
Listeria monocytogenes - genetics
Listeria monocytogenes - physiology
listeriosis
Mice
Microbiology
Molecular Sequence Data
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
protein p60
PROTEINAS
PROTEINE
Proteins
role
Sequence Homology, Amino Acid
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Summary:The major extracellular protein p60 of Listeria monocytogenes seems to be required for this microorganism's adherence to and invasion of 3T6 mouse fibroblasts but not for adherence to human epithelial Caco-2 cells. Western blot analysis with polyclonal antibodies against p60 of L. monocytogenes indicated the presence of cross-reacting proteins in the culture supernatants of all Listeria species. Protein p60 of L. monocytogenes could restore adhesion of the L. monocytogenes mutant RIII (impaired in the synthesis of p60) to mouse fibroblasts more efficiently than that of Listeria grayi. The amino acid sequences of the p60-related proteins of L. innocua, L. ivanovii, L. seeligeri, L. welshimeri, and L. grayi indicated highly conserved regions of about 120 amino acids at both the N-terminal and the C-terminal ends. The middle portions of these proteins, consisting of about 240 amino acids, varied considerably. These parts include the repeat domain consisting of repetitions of Thr (T) and Asn (N) which was present only, albeit in different arrangements, in the p60 proteins of L. monocytogenes and L. innocua. The p60-related proteins of L. grayi, L. ivanovii, L. seeligeri, and L. welshimeri each contained an insertion of 54 amino acids which was absent in the p60 proteins of L. monocytogenes and L. innocua
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.174.24.8166-8171.1992