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Conference Paper: A Novel Methodology for Isolating Broadly Neutralizing HIV-1 Human Monoclonal Antibodies

TitleA Novel Methodology for Isolating Broadly Neutralizing HIV-1 Human Monoclonal Antibodies
Authors
Issue Date2013
PublisherMary Ann Liebert, Inc Publishers. The Journal's web site is located at http://www.liebertpub.com/aid
Citation
AIDS Vaccine 2013: Progress, Partnership and Perseverance, Barcelona, Spain, 7-10 October 2013. In AIDS Research and Human Retroviruses, 2013, v. 29 n. 11, p. A-53, abstract no. P03.34 How to Cite?
AbstractBackground: Identification of broadly neutralizing HIV-1 human monoclonal antibodies (bnmAbs) may aid in development of an effective HIV-1/AIDS vaccine and antibody drugs for prevention and treatment of HIV-1 infection. Many HIV-1 bnmAbs have been identified from HIV-1-infected ‘‘elite controllers’’, especially in the past three years. Most of known bnmAbs were isolated based on their binding to HIV-1 envelope glycoprotein (Env) or engineered Envs, thus, large-scale expression and purification of isolated clones and characterization of purified soluble antibodies for neutralization breadth and potency were required, which was costly and time-consuming. Methods: Here, we developed a novel methodology for isolating HIV-1 bnmAbs based on antibody neutralization activity by displaying immune antibody libraries on target cell surface followed by sorting the cells by antibody neutralization ability to specific pseudotype virus. Results: After several rounds of sorting, a panel of human mAbs has been isolated from two ‘‘elite controllers’’ that can neutralize various isolates from clade B and clade C. Conclusion: We are currently measuring the neutralizing capability of these mAbs against different clades of virus, and expressing these mAbs as soluble form and will test them in a standardized TZM-bl neutralization assay to confirm the neutralization breadth and potency of isolated mAbs.
DescriptionPoster presentation
Abstract book is also available at the conference website
Persistent Identifierhttp://hdl.handle.net/10722/186867
ISSN
2019 Impact Factor: 1.765
2015 SCImago Journal Rankings: 1.024
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSun, Z-
dc.contributor.authorLi, J-
dc.contributor.authorShao, Y-
dc.contributor.authorZhang, M-
dc.date.accessioned2013-08-20T12:22:30Z-
dc.date.available2013-08-20T12:22:30Z-
dc.date.issued2013-
dc.identifier.citationAIDS Vaccine 2013: Progress, Partnership and Perseverance, Barcelona, Spain, 7-10 October 2013. In AIDS Research and Human Retroviruses, 2013, v. 29 n. 11, p. A-53, abstract no. P03.34-
dc.identifier.issn0889-2229-
dc.identifier.urihttp://hdl.handle.net/10722/186867-
dc.descriptionPoster presentation-
dc.descriptionAbstract book is also available at the conference website-
dc.description.abstractBackground: Identification of broadly neutralizing HIV-1 human monoclonal antibodies (bnmAbs) may aid in development of an effective HIV-1/AIDS vaccine and antibody drugs for prevention and treatment of HIV-1 infection. Many HIV-1 bnmAbs have been identified from HIV-1-infected ‘‘elite controllers’’, especially in the past three years. Most of known bnmAbs were isolated based on their binding to HIV-1 envelope glycoprotein (Env) or engineered Envs, thus, large-scale expression and purification of isolated clones and characterization of purified soluble antibodies for neutralization breadth and potency were required, which was costly and time-consuming. Methods: Here, we developed a novel methodology for isolating HIV-1 bnmAbs based on antibody neutralization activity by displaying immune antibody libraries on target cell surface followed by sorting the cells by antibody neutralization ability to specific pseudotype virus. Results: After several rounds of sorting, a panel of human mAbs has been isolated from two ‘‘elite controllers’’ that can neutralize various isolates from clade B and clade C. Conclusion: We are currently measuring the neutralizing capability of these mAbs against different clades of virus, and expressing these mAbs as soluble form and will test them in a standardized TZM-bl neutralization assay to confirm the neutralization breadth and potency of isolated mAbs.-
dc.languageeng-
dc.publisherMary Ann Liebert, Inc Publishers. The Journal's web site is located at http://www.liebertpub.com/aid-
dc.relation.ispartofAIDS Research and Human Retroviruses-
dc.rightsAIDS Research and Human Retroviruses. Copyright © Mary Ann Liebert, Inc Publishers.-
dc.titleA Novel Methodology for Isolating Broadly Neutralizing HIV-1 Human Monoclonal Antibodies-
dc.typeConference_Paper-
dc.identifier.emailLi, J: joyli@hku.hk-
dc.identifier.emailZhang, M: zhangmy@hku.hk-
dc.identifier.authorityZhang, M=rp01409-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1089/aid.2013.1500-
dc.identifier.hkuros219405-
dc.identifier.volume29-
dc.identifier.issue11-
dc.identifier.spageA-53, abstract no. P03.34-
dc.identifier.epageA-53, abstract no. P03.34-
dc.identifier.isiWOS:000326037500498-
dc.publisher.placeUnited States-

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