Abstract

The attachment of two strains of Mycoplasma bovoculi to erythrocytes was measured using 35S-methionine-labelled organisms. Receptor sites of M. bovoculi involved in this attachment are trypsin-sensitive, since mild trypsin treatment of the intact organisms abolished this process completely. Pretreatment of erythrocytes with trypsin or increasing concentrations of neuraminidase resulted in no measurable effect. Monoclonal antibody MA25.5 directed against a M. bovoculi surface antigen of 94 kDa termed p94 blocked 40% of the attachment, while MA18.13 directed against a 57 kDa protein band of M. bovoculi had no effect on the attachment process. Other properties of M. bovoculi were tested using six strains of the mycoplasma and erythrocytes from several animal species. None of the strains showed haemagglutinating or haemadsorbing activities.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.