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987P fimbriae from porcine enterotoxigenic Escherichia coli : Characterization, N‐terminal amino acid sequence and immunization with purified antigen
Author(s) -
Pedersen Jesper K.,
Klemm Per,
Gaastra Wim
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01277.x
Subject(s) - enterotoxigenic escherichia coli , fimbria , escherichia coli , antigen , peptide sequence , immunization , microbiology and biotechnology , biology , enterobacteriaceae , sequence (biology) , chemistry , biochemistry , enterotoxin , gene , genetics
The 987P fimbrial antigen was purified from a spontaneous overproducing variant. The protein was characterized with respect to M r , amino acid sequence and partial covalent structure. The purified protein was used for vaccination trials, and excellent protection of piglets upon challenge with 987P positive enterotoxigenic strains was seen.

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