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Journal of Virology, January 2009, p. 396-407, Vol. 83, No. 1
0022-538X/09/$08.00+0     doi:10.1128/JVI.01170-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Kaposi's Sarcoma-Associated Herpesvirus gH/gL: Glycoprotein Export and Interaction with Cellular Receptors{triangledown}

Alexander Hahn,1 Alexander Birkmann,1,{ddagger} Effi Wies,1 Dominik Dorer,1,{dagger} Kerstin Mahr,2 Michael Stürzl,3 Fritz Titgemeyer,2,4 and Frank Neipel1*

Virologisches Institut, Universität Erlangen-Nürnberg, Schlossgarten 4, D-91054 Erlangen, Germany,1 Lehrstuhl für Mikrobiologie, Universität Erlangen-Nürnberg, Staudtstr. 5, D-91058 Erlangen, Germany,2 Chirurgische Klinik, Abteilung für Molekulare und Experimentelle Chirurgie, Universität Erlangen-Nürnberg, Schwabachanlage 10, D-91054 Erlangen, Germany,3 Department of Oecotrophology, University of Applied Sciences Münster, Corrensstr. 25, 48149 Münster, Germany4

Received 5 June 2008/ Accepted 20 October 2008

The attachment, entry, and fusion of Kaposi's sarcoma-associated herpesvirus (KSHV) with target cells are mediated by complex machinery containing, among others, viral glycoprotein H (gH) and its alleged chaperone, gL. We observed that KSHV gH, in contrast to its homologues in several other herpesviruses, is transported to the cytoplasm membrane independently from gL, but not vice versa. Mutational analysis revealed that the N terminus of gH is sufficient for gL interaction. However, the entire extracellular part of gH is required for efficient gL secretion. The soluble ectodomain of gH was sufficient to interact with the surfaces of potential target cells in a heparin-dependent manner, and binding was further enhanced by coexpression of gL. Surface plasmon resonance revealed a remarkably high affinity of gH for glycosaminoglycans. Heparan sulfate (HS) proteoglycans of the syndecan family act as cellular receptors for the gH/gL complex. They promoted KSHV infection, and expression of gH/gL on target cells inhibited subsequent KSHV infection. Whereas gH alone was able to bind to HS, we observed that only the gH/gL complex adhered to heparan sulfate-negative cells at lamellipodium-like structures.

* Corresponding author. Mailing address: Virologisches Institut, Universität Erlangen-Nürnberg, Schloßgarten 4, D-91054 Erlangen, Germany. Phone: 49-9131-8523786. Fax: 49-9131-8526493. E-mail: Frank.neipel{at}viro.med.uni-erlangen.de

{triangledown} Published ahead of print on 22 October 2008.

{ddagger} Present address: AiCuris GmbH, Friedrich-Ebert-Str. 415, 42117 Wuppertal, Germany.

{dagger} Present address: Helmholtz-University Group Oncolytic Adenoviruses, German Cancer Research Center (DKFZ), and Department of Dermatology, University of Heidelberg, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany.

Journal of Virology, January 2009, p. 396-407, Vol. 83, No. 1
0022-538X/09/$08.00+0     doi:10.1128/JVI.01170-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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