期刊
CELLULAR MICROBIOLOGY
卷 15, 期 11, 页码 1818-1836出版社
WILEY
DOI: 10.1111/cmi.12150
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资金
- German Science Foundation (DFG) [SCHE 1552/2-1]
- Portuguese Foundation for Science and Technology [SFRH/BD/45921/2008]
- UK Research Councils' Basic Technology Initiative Glycoarrays' [GRS/79268]
- EPSRC [EP/G037604/1]
- Wellcome Trust [WT093378MA]
- NCI Alliance of Glycobiologists for Detection of Cancer and Cancer Risk [U01 CA128416]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/45921/2008] Funding Source: FCT
- Engineering and Physical Sciences Research Council [EP/G037604/1, GR/S79268/02] Funding Source: researchfish
- EPSRC [EP/G037604/1] Funding Source: UKRI
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 withheparin-like' domains of cellular HSPGs. We propose that HS sequences with specific sulfation patterns are required to facilitate HPV-16 infection.
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