TY - JOUR
T1 - Isolation of a mannose-specific lectin from Escherichia coli and its role in the adherence of the bacteria to epithelial cells
AU - Eshdat, Yuval
AU - Ofek, Itzhak
AU - Yashouv-Gan, Yehudit
AU - Sharon, Nathan
AU - Mirelman, David
N1 - Funding Information:
This study was supported in part by grants from the Foundation for the Advancement of Mankind, Jerusalem (to N.S.) and the Rockefeller Foundation (to D.M.). N.S. is an Established Investigator of the Chief Scientist's Bureau of the Israel Ministry of Health,
PY - 1978/12/29
Y1 - 1978/12/29
N2 - A high molecular weight protein aggregate, which agglutinates yeast cells, human epithelial cells and mouse lymphocytes, was isolated from extracts of Escherichia coli by differential centrifugation and gel filtration. The agglutination is specifically inhibited by d-mannose and its derivatives, the best inhibitor being p-nitrophenyl α-d-mannoside. Sodium dodecyl sulfate gel electrophoresis showed that the lectin consists of protein subunits with identical Mr of ∼36500. The amino acid composition of the purified lectin is different from that reported for the type I pili protein, the K99 antigen and the major outer membrane protein Ia of E. coli. The protein appears to be located on the bacterial surface, and is probably involved in the mannose-specific adherence of E. coli to eukaryotic cells.
AB - A high molecular weight protein aggregate, which agglutinates yeast cells, human epithelial cells and mouse lymphocytes, was isolated from extracts of Escherichia coli by differential centrifugation and gel filtration. The agglutination is specifically inhibited by d-mannose and its derivatives, the best inhibitor being p-nitrophenyl α-d-mannoside. Sodium dodecyl sulfate gel electrophoresis showed that the lectin consists of protein subunits with identical Mr of ∼36500. The amino acid composition of the purified lectin is different from that reported for the type I pili protein, the K99 antigen and the major outer membrane protein Ia of E. coli. The protein appears to be located on the bacterial surface, and is probably involved in the mannose-specific adherence of E. coli to eukaryotic cells.
UR - http://www.scopus.com/inward/record.url?scp=0018246145&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(78)91179-8
DO - 10.1016/0006-291X(78)91179-8
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AN - SCOPUS:0018246145
SN - 0006-291X
VL - 85
SP - 1551
EP - 1559
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -