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Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5
SERINC5 is a multi-pass transmembrane protein that is thought to play a role in serine incorporation during cellular membrane biosynthesis. This protein has also been identified as a human immunodeficiency virus Type 1 (HIV-1) restriction factor. The paucity of monoclonal antibodies (mAbs) against S...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7531522/ https://www.ncbi.nlm.nih.gov/pubmed/32835602 http://dx.doi.org/10.1080/19420862.2020.1802187 |
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author | Molnar, Sebastian Wieczorek, Lindsay Zemil, Michelle Schulte, Bianca Martinez, Elizabeth Gift, Syna Tang, Lan Streeck, Hendrik Gramzinski, Robert A. Michael, Nelson L. Joyce, Gordon Polonis, Victoria R. |
author_facet | Molnar, Sebastian Wieczorek, Lindsay Zemil, Michelle Schulte, Bianca Martinez, Elizabeth Gift, Syna Tang, Lan Streeck, Hendrik Gramzinski, Robert A. Michael, Nelson L. Joyce, Gordon Polonis, Victoria R. |
author_sort | Molnar, Sebastian |
collection | PubMed |
description | SERINC5 is a multi-pass transmembrane protein that is thought to play a role in serine incorporation during cellular membrane biosynthesis. This protein has also been identified as a human immunodeficiency virus Type 1 (HIV-1) restriction factor. The paucity of monoclonal antibodies (mAbs) against SERINC5 has posed a challenge for the study of the endogenous protein. Here we report the development of novel anti-SERINC5 mAbs that target three distinct loops on the protein. We demonstrate that these SERINC5 mAbs can be used to detect endogenously expressed SERINC5 protein in various cell lines using Western blot, whole-cell ELISA, flow cytometry, and immunocytochemistry. We further show that some of these antibodies can detect SERINC5 that is present in HIV-1 viral stocks. These antibodies will aid in the characterization of the functions and mechanisms of action of SERINC5 in different cell types. |
format | Online Article Text |
id | pubmed-7531522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-75315222020-10-13 Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 Molnar, Sebastian Wieczorek, Lindsay Zemil, Michelle Schulte, Bianca Martinez, Elizabeth Gift, Syna Tang, Lan Streeck, Hendrik Gramzinski, Robert A. Michael, Nelson L. Joyce, Gordon Polonis, Victoria R. MAbs Report SERINC5 is a multi-pass transmembrane protein that is thought to play a role in serine incorporation during cellular membrane biosynthesis. This protein has also been identified as a human immunodeficiency virus Type 1 (HIV-1) restriction factor. The paucity of monoclonal antibodies (mAbs) against SERINC5 has posed a challenge for the study of the endogenous protein. Here we report the development of novel anti-SERINC5 mAbs that target three distinct loops on the protein. We demonstrate that these SERINC5 mAbs can be used to detect endogenously expressed SERINC5 protein in various cell lines using Western blot, whole-cell ELISA, flow cytometry, and immunocytochemistry. We further show that some of these antibodies can detect SERINC5 that is present in HIV-1 viral stocks. These antibodies will aid in the characterization of the functions and mechanisms of action of SERINC5 in different cell types. Taylor & Francis 2020-08-23 /pmc/articles/PMC7531522/ /pubmed/32835602 http://dx.doi.org/10.1080/19420862.2020.1802187 Text en This work was authored as part of the Contributor’s official duties as an Employee of the United States Government and is therefore a work of the United States Government. In accordance with 17 U.S.C. 105, no copyright protection is available for such works under U.S. Law. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) ), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Report Molnar, Sebastian Wieczorek, Lindsay Zemil, Michelle Schulte, Bianca Martinez, Elizabeth Gift, Syna Tang, Lan Streeck, Hendrik Gramzinski, Robert A. Michael, Nelson L. Joyce, Gordon Polonis, Victoria R. Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title | Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title_full | Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title_fullStr | Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title_full_unstemmed | Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title_short | Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous and virion-associated SERINC5 |
title_sort | novel monoclonal antibodies to the serinc5 hiv-1 restriction factor detect endogenous and virion-associated serinc5 |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7531522/ https://www.ncbi.nlm.nih.gov/pubmed/32835602 http://dx.doi.org/10.1080/19420862.2020.1802187 |
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