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Infection and Immunity, September 2000, p. 4872-4876, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Coincubation of Human Spermatozoa with Chlamydia trachomatis In Vitro Causes Increased Tyrosine Phosphorylation of Sperm Proteins

S. Hosseinzadeh,1 I. A. Brewis,2,3 A. A. Pacey,3 H. D. M. Moore,2,3 and A. Eley1,*

Division of Molecular and Genetic Medicine, The Medical School, The University of Sheffield, Sheffield, S10 2RX,1 Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, S10 2TN,2 and University Department of Obstetrics and Gynaecology, Jessop Hospital for Women, Sheffield, S3 7RE,3 United Kingdom

Received 7 February 2000/Returned for modification 22 March 2000/Accepted 30 May 2000

Elementary bodies (EBs) of the obligate intracellular bacterium Chlamydia trachomatis are responsible for the first step of attachment to host cells. We have studied the effects of EBs on human sperm protein tyrosine phosphorylation, which is important to sperm function. Indirect immunofluorescence using antiphosphotyrosine antibodies showed that serovar E, but not LGV, caused increased tyrosine phosphorylation which was localized to the sperm tail region. Immunoblotting revealed that serovar E caused a marked increase in tyrosine phosphorylation of 80- and 95-kDa sperm proteins, whereas serovar LGV caused increased phosphorylation of only the 80-kDa moiety. Considering the importance of tyrosine phosphorylation for sperm capacitation and other aspects of sperm function, we conclude that EBs may affect these events.

* Corresponding author. Mailing address: Division of Molecular and Genetic Medicine, The Medical School, The University of Sheffield, Sheffield, S10 2RX, United Kingdom. Phone: 44 (0) 114 272 4072. Fax: 44 (0) 114 273 9926. E-mail: a.r.eley{at}sheffield.ac.uk.

Infection and Immunity, September 2000, p. 4872-4876, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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