This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yavlovich, A. Articles by Rottem, S. Search for Related Content PubMed PubMed Citation Articles by Yavlovich, A. Articles by Rottem, S. Pubmed/NCBI databases Gene GEO Profiles HomoloGene UniGene Compound via MeSH Substance via MeSH Hazardous Substances DB CHOLESTEROL

 Previous Article  |  Next Article 

Infection and Immunity, September 2004, p. 5004-5011, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5004-5011.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Mycoplasma fermentans Binds to and Invades HeLa Cells: Involvement of Plasminogen and Urokinase

Amichai Yavlovich,¹ Avigail Katzenell,¹ Mark Tarshis,¹ Abd A.-R. Higazi,² and Shlomo Rottem^1*

Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School,¹ Department of Clinical Biochemistry-Hadassah Hospital, Mount Scopus, Jerusalem, Israel²

Received 10 October 2003/ Returned for modification 27 April 2004/ Accepted 3 June 2004

Adherence of Mycoplasma fermentans to HeLa cells followed saturation kinetics, required a divalent cation, and was enhanced by preincubation of the organism at 37°C for 1 h in a low-osmolarity solution. Proteolytic digestion, choline phosphate, or anti-choline phosphate antibodies partially inhibited the adherence, supporting the notion that M. fermentans utilizes at least two surface components for adhesion, a protease-sensitive surface protein and a phosphocholine-containing glycolipid. Plasminogen binding to M. fermentans greatly increased the maximal adherence of the organism to HeLa cells. Anti-plasminogen antibodies and free plasminogen inhibited this increase. These observations suggest that in the presence of plasminogen the organism adheres to novel sites on the HeLa cell surface, which are apparently plasminogen receptors. Plasminogen-bound M. fermentans was detected exclusively on the cell surface of the infected HeLa cells. Nevertheless, plasminogen binding in the presence of the urokinase-type plasminogen activator (uPA) promoted the invasion of HeLa cells by M. fermentans. The latter finding indicates that the invasiveness of M. fermentans does not result from binding plasminogen but from activation of the bound plasminogen to plasmin. Cholesterol depletion and sequestration with ß-cyclodextrin and filipin, respectively, did not affect the capacity of M. fermentans to adhere, but invasion of HeLa cells by uPA-activated plasminogen-bound M. fermentans was impaired, suggesting that lipid rafts are implicated in M. fermentans entry.

---

* Corresponding author. Mailing address: Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel. Phone: (972) 2-6758148. Fax: (972) 2-6438205. E-mail: rottem{at}cc.huji.ac.il.

Editor: V. J. DiRita

---

Infection and Immunity, September 2004, p. 5004-5011, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5004-5011.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Yavlovich, A., Rechnitzer, H., Rottem, S. (2007). {alpha}-Enolase Resides on the Cell Surface of Mycoplasma fermentans and Binds Plasminogen. Infect. Immun. 75: 5716-5719 [Abstract] [Full Text]