Open AccessComparison of the abilities of proteins from Bartonella bacilliformis and Bartonella henselae to deform red cell membranes and to bind to red cell ghost proteins
Author(s) -
IwakiEgawa Sachiko,
Ihler Garret M
Publication year - 1997
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.1574-6968.1997.tb12775.x
Subject(s) - bartonella henselae , biology , bacterial outer membrane , bartonella , spectrin , membrane protein , microbiology and biotechnology , cytoskeleton , cell , biochemistry , membrane , genetics , escherichia coli , gene , antibody , serology
Infections in humans by Bartonella bacilliformis , but not Bartonella henselae , are characterized by invasion of red cells. Supernatants of culture medium from B. bacilliformis and B. henselae each contain a protein which causes invagination of membranes of human red cells and formation of intracellular vacuoles. These two proteins are very similar in molecular mass, heat stability and mechanism of action. B. henselae does not bind to human red cells, but human red cell ghost membrane proteins were recognized by both bacteria, five by B. bacilliformis and the same five, and one additional protein by B. henselae . Two of these proteins had molecular masses consistent with actin and spectrin. Actin binds to five electroblotted outer membrane proteins from B. henselae and four of these proteins are retained on an actin‐Sepharose column.