Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding

Human papillomaviruses (HPVs) are the cause of epithelial lesions, HPV type 16 and type 18 being associated with the development of anogenital cancer. The L1 Major Capsid Protein (L1) represents about 90% of total HPV protein and is involved in virus?host cell interaction, but little is known about...

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Tipo de recurso:
Fecha de publicación:
2003
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/25927
Acceso en línea:
https://doi.org/10.1002/ijc.11433
https://repository.urosario.edu.co/handle/10336/25927
Palabra clave:
L1 major capsid protein
Peptide
Human papillomavirus
Specific binding
VLPs
Rights
License
Abierto (Texto Completo)
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oai_identifier_str oai:repository.urosario.edu.co:10336/25927
network_acronym_str EDOCUR2
network_name_str Repositorio EdocUR - U. Rosario
repository_id_str
spelling 0ad382b4-d6b1-4878-a4a1-bd78fc45e107-1dd3af730-1a89-42fc-a5de-64665dc12a41-1a650efd0-af5f-4ce9-9620-e1cad93a9173-1ef6547b6-3130-435a-8a09-7ca050cd7b64-1eba5265c-2b9f-49a4-8c8c-4e3459a41e19-15e82e691-ba88-4d28-b934-b924d1350834-191225589-1d7acca3a-ee59-4f6f-9a8d-0b812932d115-14272869d-a644-44e9-a7a4-9c26d936bb9e-11450e86b-c3ae-413a-bffa-4caa6fae204a-1abafc44c-40e3-4a62-9de8-e76e8c4c1178-1bc380284-d23e-4afd-ad07-efa220c5bd4b-16d410cb9-4386-458d-9db3-1fd047cafed9-1d264de78-ef26-4502-8d81-0af1121844bc-186890999-9e21-438a-8c2a-58b45684be07-110ecd4f9-843f-4ef2-bec0-7d39d3381a13-1518488266002020-08-06T16:20:14Z2020-08-06T16:20:14Z2003-09-17Human papillomaviruses (HPVs) are the cause of epithelial lesions, HPV type 16 and type 18 being associated with the development of anogenital cancer. The L1 Major Capsid Protein (L1) represents about 90% of total HPV protein and is involved in virus?host cell interaction, but little is known about this binding process. L1 sequences from HPV types 16 and 18 were synthesized in 56 20?mer peptides, covering the entire protein, HPLC?purified, 125I?radiolabeled and tested in VERO and HeLa cell?binding assays to identify those peptides with high specific binding activity. Peptides 18283 (residues 54–77) and 18294 (274–308) from HPV16 L1, as well as 18312 (59–78) and 18322 (259–278) from HPV18 L1, presented high specific target cell binding activity. Peptide 18283 and 18294 affinity constants were 300 and 600 nM, respectively. Enzyme cell treatment before binding assay indicated that VERO and HeLa cell peptide receptor is a surface?exposed protein. There was a 60% reduction in peptide 18283 binding to heparin lyase?treated cells. Cross?linking assays showed that these proteins molecular weights were around 69 and 54 kDa. Peptides 18283 and 18294 specifically inhibited HPV?16 VLP binding to HeLa cells. According to the L1? and VLP?reported structure, both peptides are close on the VLP?surface, belonging to the outer surface broad pockets suggested as being potential receptor sites. Furthermore, it has been reported that a conserved motif from peptide 18294 is the target for neutralizing antibodies. These results suggest that such binding sequences are used by the virus as cell?binding regions.application/pdfhttps://doi.org/10.1002/ijc.11433ISSN?: ?0020-7136EISSN: 1097-0215https://repository.urosario.edu.co/handle/10336/25927engJohn Wiley and Sons424No. 3416International Journal of CancerVol. 107International Journal of Cancer, ISSN?: ?0020-7136;EISSN: 1097-0215, Vol.107, No.3 (November, 2003); pp.416-424https://onlinelibrary.wiley.com/doi/full/10.1002/ijc.11433Abierto (Texto Completo)http://purl.org/coar/access_right/c_abf2International Journal of Cancerinstname:Universidad del Rosarioreponame:Repositorio Institucional EdocURL1 major capsid proteinPeptideHuman papillomavirusSpecific bindingVLPsHuman papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs bindingLa unión del péptido de la proteína L1 del virus del papiloma humano tipo 16 y 18 a las células VERO y HeLa inhibe la unión de sus VLParticleArtículohttp://purl.org/coar/version/c_970fb48d4fbd8a85http://purl.org/coar/resource_type/c_6501Vera?Bravo, RicardoUrquiza, MauricioGarcía, Javier E.Rodríguez, Luis E.Puentes, AlvaroLópez, RamsesCurtidor, HernandoSuárez, Jorge E.Torres, ElizabethGuzmán, FannyDíaz , DianaCortes, JimenaBravo, María M.Cómbita, Alba L.Orozco, OscarPatarroyo, Manuel E.Ocampo, Marisol10336/25927oai:repository.urosario.edu.co:10336/259272021-06-03 00:50:21.039https://repository.urosario.edu.coRepositorio institucional EdocURedocur@urosario.edu.co
dc.title.spa.fl_str_mv Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
dc.title.TranslatedTitle.spa.fl_str_mv La unión del péptido de la proteína L1 del virus del papiloma humano tipo 16 y 18 a las células VERO y HeLa inhibe la unión de sus VLP
title Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
spellingShingle Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
L1 major capsid protein
Peptide
Human papillomavirus
Specific binding
VLPs
title_short Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
title_full Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
title_fullStr Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
title_full_unstemmed Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
title_sort Human papillomavirus type 16 and 18 L1 protein peptide binding to VERO and HeLa cells inhibits their VLPs binding
dc.subject.keyword.spa.fl_str_mv L1 major capsid protein
Peptide
Human papillomavirus
Specific binding
VLPs
topic L1 major capsid protein
Peptide
Human papillomavirus
Specific binding
VLPs
description Human papillomaviruses (HPVs) are the cause of epithelial lesions, HPV type 16 and type 18 being associated with the development of anogenital cancer. The L1 Major Capsid Protein (L1) represents about 90% of total HPV protein and is involved in virus?host cell interaction, but little is known about this binding process. L1 sequences from HPV types 16 and 18 were synthesized in 56 20?mer peptides, covering the entire protein, HPLC?purified, 125I?radiolabeled and tested in VERO and HeLa cell?binding assays to identify those peptides with high specific binding activity. Peptides 18283 (residues 54–77) and 18294 (274–308) from HPV16 L1, as well as 18312 (59–78) and 18322 (259–278) from HPV18 L1, presented high specific target cell binding activity. Peptide 18283 and 18294 affinity constants were 300 and 600 nM, respectively. Enzyme cell treatment before binding assay indicated that VERO and HeLa cell peptide receptor is a surface?exposed protein. There was a 60% reduction in peptide 18283 binding to heparin lyase?treated cells. Cross?linking assays showed that these proteins molecular weights were around 69 and 54 kDa. Peptides 18283 and 18294 specifically inhibited HPV?16 VLP binding to HeLa cells. According to the L1? and VLP?reported structure, both peptides are close on the VLP?surface, belonging to the outer surface broad pockets suggested as being potential receptor sites. Furthermore, it has been reported that a conserved motif from peptide 18294 is the target for neutralizing antibodies. These results suggest that such binding sequences are used by the virus as cell?binding regions.
publishDate 2003
dc.date.created.spa.fl_str_mv 2003-09-17
dc.date.accessioned.none.fl_str_mv 2020-08-06T16:20:14Z
dc.date.available.none.fl_str_mv 2020-08-06T16:20:14Z
dc.type.eng.fl_str_mv article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.spa.spa.fl_str_mv Artículo
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1002/ijc.11433
dc.identifier.issn.none.fl_str_mv ISSN?: ?0020-7136
EISSN: 1097-0215
dc.identifier.uri.none.fl_str_mv https://repository.urosario.edu.co/handle/10336/25927
url https://doi.org/10.1002/ijc.11433
https://repository.urosario.edu.co/handle/10336/25927
identifier_str_mv ISSN?: ?0020-7136
EISSN: 1097-0215
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.citationEndPage.none.fl_str_mv 424
dc.relation.citationIssue.none.fl_str_mv No. 3
dc.relation.citationStartPage.none.fl_str_mv 416
dc.relation.citationTitle.none.fl_str_mv International Journal of Cancer
dc.relation.citationVolume.none.fl_str_mv Vol. 107
dc.relation.ispartof.spa.fl_str_mv International Journal of Cancer, ISSN?: ?0020-7136;EISSN: 1097-0215, Vol.107, No.3 (November, 2003); pp.416-424
dc.relation.uri.spa.fl_str_mv https://onlinelibrary.wiley.com/doi/full/10.1002/ijc.11433
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.acceso.spa.fl_str_mv Abierto (Texto Completo)
rights_invalid_str_mv Abierto (Texto Completo)
http://purl.org/coar/access_right/c_abf2
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv John Wiley and Sons
dc.source.spa.fl_str_mv International Journal of Cancer
institution Universidad del Rosario
dc.source.instname.none.fl_str_mv instname:Universidad del Rosario
dc.source.reponame.none.fl_str_mv reponame:Repositorio Institucional EdocUR
repository.name.fl_str_mv Repositorio institucional EdocUR
repository.mail.fl_str_mv edocur@urosario.edu.co
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