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- Title
Heparin increases the infectivity of Human Papillomavirus Type 16 independent of cell surface proteoglycans and induces L1 epitope exposure.
- Authors
Cerqueira, Carla; Liu, Yan; Kühling, Lena; Chai, Wengang; Hafezi, Wali; Kuppevelt, Toin H.; Kühn, Joachim E.; Feizi, Ten; Schelhaas, Mario
- Abstract
Human Papillomaviruses ( HPVs) are the etiological agents of cervical cancer, and HPV-16 is the most prevalent type. Several HPVs require heparan sulfate proteoglycans ( HSPGs) for cell binding. Here, we analyse the phenomenon that preincubation of HPV-16 with increasing concentrations of heparin results in partial restoration rather than more efficient inhibition of infection. While corroborating that the HSPGs are cell-binding receptors for HPV-16, heparin-preincubated virus bound to the extracellular matrix ( ECM) via laminin-332. Furthermore, the interaction of virions with heparin, a representative of the highly sulfated S-domains of heparan sulfate ( HS) chains of HSPGs, allowed HPV-16 infection in the absence of cell surface HSPGs. Therefore, we concluded that specific glycan moieties but not specific HSPG protein backbones are required for infection. The increased binding of an epitope-specific antibody to the viral capsid after heparin binding suggested that initial conformational changes in the HPV-16 virion occur during infection by interaction with'heparin-like' domains of cellular HSPGs. We propose that HS sequences with specific sulfation patterns are required to facilitate HPV-16 infection.
- Subjects
HEPARIN; HUMAN papillomavirus vaccines; MEMBRANE glycoproteins; EPITOPES; CERVICAL cancer; HEPARAN sulfate proteoglycans; EXTRACELLULAR matrix; LAMININS
- Publication
Cellular Microbiology, 2013, Vol 15, Issue 11, p1818
- ISSN
1462-5814
- Publication type
Article
- DOI
10.1111/cmi.12150