Comparison of the abilities of proteins from Bartonella bacilliformis and Bartonella henselae to deform red cell membranes and to bind to red cell ghost proteins.
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.
Iwaki-Egawa
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Department of Medical Biochemistry and Genetics, College of Medicine, TAMU Health Science Center, College Station 77843-1114, USA.
Ihler
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GM
D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism; D001474:Bartonella Infections / Q000378:metabolism*; D018416:Bartonella henselae / Q000737:chemistry*; D004730:Endothelium, Vascular / Q000737:chemistry / Q000378:metabolism / Q000382:microbiology; D004907:Erythrocyte Deformability; D004910:Erythrocyte Membrane / Q000737:chemistry / Q000378:metabolism / Q000382:microbiology*; D006801:Humans; D011485:Protein Binding; D013045:Species Specificity; D014471:Umbilical Veins / Q000166:cytology
D001426:Bacterial Proteins