Identification and partial characterization of a cytolytic toxin produced by Gardnerella vaginalis

Author:

Rottini G1,Dobrina A1,Forgiarini O1,Nardon E1,Amirante G A1,Patriarca P1

Affiliation:

1. Institute of General Pathology, University of Trieste, Italy.

Abstract

Generation and release into the culture medium of a cytolytic toxin by Gardnerella vaginalis has been demonstrated. Addition of starch and of the nonionic detergent Tween 80 to the culture medium was essential to recover cytolytic activity. A protein with an apparent molecular mass of 61 to 63 kDa was purified from the culture supernatants showing lytic activity towards erythrocytes and nucleated cells, such as human endothelial cells and human neutrophils. The protein had marked selectivity for human erythrocytes, while erythrocytes from other species were not lysed or were lysed at much higher concentrations of the protein than those needed for human erythrocytes. The cytolytic activity was remarkably unstable in polar media, but was stabilized by nonionic detergents, by binding, or by insertion into the target cell membrane, suggesting its amphiphilic nature.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference38 articles.

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4. Copurification of Leptospira interrogans, serovar pomona hemolysin and sphingomyelinase C;Bernheimer A. W.;Infect. Immun.,1986

5. Interaction between membranes and cytolytic peptides;Bernheimer A. W.;Biochim. Biophys. Acta,1986

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