Contact-dependent hemolytic activity distinct from deforming activity of Bartonella bacilliformis.
Although Bartonella bacilliformis causes a severe anemia in humans, this study presents the first report of hemolytic activity by B. bacilliformis. The activity was not apparent in culture supernatants but was reliably detected when B. bacilliformis cells were centrifuged onto erythrocytes prior to incubation. Abrogation of hemolytic activity by proteinase K treatment suggested the hemolysin was a Bartonella protein. Even though hemolysis required relatively long incubation times, de novo protein synthesis was not required to produce the protein. A preparation containing factors released by B. bacilliformis, including deformin, a B. bacilliformis protein able to induce pits and invaginations in erythrocyte membranes, had some ability to lyse erythrocytes. However, pre-deformed erythrocytes did not lyse faster or to a greater extent than control erythrocytes after the addition of B. bacilliformis cells. Inhibition of deformation caused by B. bacilliformis cells with the erythrocyte ATPase inhibitor, vanadate, did not affect hemolytic activity. This study suggests hemolytic activity and deforming activity are attributable to different B. bacilliformis proteins.
Hendrix
L R
LR
Department of Medical Microbiology and Immunology, Texas A&M University System Health Science Center, College Station, TX 77843-1114, USA. lhendrix@tamu.edu
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001473:Bartonella / Q000254:growth & development / Q000472:pathogenicity*; D019286:Endopeptidase K / Q000378:metabolism; D004912:Erythrocytes / Q000382:microbiology*; D006460:Hemolysin Proteins / Q000378:metabolism*; D006461:Hemolysis; D006801:Humans; D014638:Vanadates / Q000494:pharmacology
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; C092807:deformin protein, Bartonella bacilliformis; D014638:Vanadates; D019286:Endopeptidase K