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dc.contributor.authorCruikshank, William W.
dc.contributor.authorDoctrow, Susan R.
dc.contributor.authorFalvo, Melissa S.
dc.contributor.authorHuffman, Karl
dc.contributor.authorMaciaszek, Joseph Walter
dc.contributor.authorViglianti, Gregory A.
dc.contributor.authorRaina, Jay
dc.contributor.authorKornfeld, Hardy
dc.contributor.authorMalfroy, Bernard
dc.date2022-08-11T08:08:56.000
dc.date.accessioned2022-08-23T16:13:17Z
dc.date.available2022-08-23T16:13:17Z
dc.date.issued1997-03-01
dc.date.submitted2008-08-29
dc.identifier.citationJ Acquir Immune Defic Syndr Hum Retrovirol. 1997 Mar 1;14(3):193-203.
dc.identifier.issn1077-9450 (Print)
dc.identifier.pmid9117450
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33586
dc.description.abstractWe have developed a chemical modification of antibodies, lipidation, which enables their intracellular delivery into living cells. Intracellular localization of lipidated antibodies was demonstrated by confocal microscopy and by measuring cellular uptake of 125I-labeled lipidated antibodies. Functionally, a lipidated monoclonal antibody directed against the Tat protein from human immunodeficiency virus type 1 (HIV-1) inhibited viral replication of several HIV-1 isolates by approximately 85% as shown by increased viability of infected cells and decreased reverse transcriptase activity. The antibody in its native form had no such effect. These data show that lipidated antibodies can reach and functionally inhibit intracellular targets. Lipidation may help to facilitate the development of intracellular immunotherapy for AIDS.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9117450&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://ovidsp.ovid.com/ovidweb.cgi?T=JS&CSC=Y&NEWS=N&PAGE=fulltext&AN=00042560-199703010-00001&LSLINK=80&D=ovft
dc.subjectAntibodies, Monoclonal; Biological Transport; Cells, Cultured; Enzyme-Linked Immunosorbent Assay; Gene Products, tat; Glycine; HIV Antibodies; HIV Core Protein p24; HIV Reverse Transcriptase; HIV-1; Immunoglobulin G; Lipoproteins; Lymphocytes; Microscopy, Fluorescence; Virus Latency; Virus Replication; tat Gene Products, Human Immunodeficiency Virus
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA lipidated anti-Tat antibody enters living cells and blocks HIV-1 viral replication
dc.typeJournal Article
dc.source.journaltitleJournal of acquired immune deficiency syndromes and human retrovirology : official publication of the International Retrovirology Association
dc.source.volume14
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/256
dc.identifier.contextkey609999
html.description.abstract<p>We have developed a chemical modification of antibodies, lipidation, which enables their intracellular delivery into living cells. Intracellular localization of lipidated antibodies was demonstrated by confocal microscopy and by measuring cellular uptake of 125I-labeled lipidated antibodies. Functionally, a lipidated monoclonal antibody directed against the Tat protein from human immunodeficiency virus type 1 (HIV-1) inhibited viral replication of several HIV-1 isolates by approximately 85% as shown by increased viability of infected cells and decreased reverse transcriptase activity. The antibody in its native form had no such effect. These data show that lipidated antibodies can reach and functionally inhibit intracellular targets. Lipidation may help to facilitate the development of intracellular immunotherapy for AIDS.</p>
dc.identifier.submissionpathgsbs_sp/256
dc.contributor.departmentDepartment of Medicine, Division of Pulmonary, Allergy & Critical Care
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages193-203


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