Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous andvirion-associated SERINC5

Sebastian Molnar; Lindsay Wieczorek; Michelle Zemil; Bianca Schulte; Elizabeth Martinez; Syna Gift; Lan Tang; Hendrik Streeck; Robert A. Gramzinski; Nelson L. Michael; Gordon Joyce; Victoria R. Polonis

doi:10.1080/19420862.2020.1802187

Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous andvirion-associated SERINC5

Sebastian Molnar, Lindsay Wieczorek, Michelle Zemil, Bianca Schulte, Elizabeth Martinez, Syna Gift, Lan Tang, Hendrik Streeck, Robert A. Gramzinski, Nelson L. Michael, Gordon Joyce, Victoria R. Polonis^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

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.

Original language	English
Article number	1802187
Journal	mAbs
Volume	12
Issue number	1
DOIs	https://doi.org/10.1080/19420862.2020.1802187
State	Published - 1 Jan 2020
Externally published	Yes

Keywords

HIV-1 restriction factor
SERINC5
immunocytochemistry
monoclonal antibody
multi-pass transmembrane protein
serine incorporator
virus capture

Access to Document

10.1080/19420862.2020.1802187

Cite this

@article{deeac1b41a9e47a89158d726d1695c75,

title = "Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous andvirion-associated SERINC5",

abstract = "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.",

keywords = "HIV-1 restriction factor, SERINC5, immunocytochemistry, monoclonal antibody, multi-pass transmembrane protein, serine incorporator, virus capture",

author = "Sebastian Molnar and Lindsay Wieczorek and Michelle Zemil and Bianca Schulte and Elizabeth Martinez and Syna Gift and Lan Tang and Hendrik Streeck and Gramzinski, {Robert A.} and Michael, {Nelson L.} and Gordon Joyce and Polonis, {Victoria R.}",

note = "Publisher Copyright: {\textcopyright} This work was authored as part of the Contributor{\textquoteright}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.",

year = "2020",

month = jan,

day = "1",

doi = "10.1080/19420862.2020.1802187",

language = "English",

volume = "12",

journal = "mAbs",

issn = "1942-0862",

number = "1",

}

TY - JOUR

T1 - Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous andvirion-associated SERINC5

AU - Molnar, Sebastian

AU - Wieczorek, Lindsay

AU - Zemil, Michelle

AU - Schulte, Bianca

AU - Martinez, Elizabeth

AU - Gift, Syna

AU - Tang, Lan

AU - Streeck, Hendrik

AU - Gramzinski, Robert A.

AU - Michael, Nelson L.

AU - Joyce, Gordon

AU - Polonis, Victoria R.

N1 - Publisher Copyright: © 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.

PY - 2020/1/1

Y1 - 2020/1/1

N2 - 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.

AB - 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.

KW - HIV-1 restriction factor

KW - SERINC5

KW - immunocytochemistry

KW - monoclonal antibody

KW - multi-pass transmembrane protein

KW - serine incorporator

KW - virus capture

UR - http://www.scopus.com/inward/record.url?scp=85089740550&partnerID=8YFLogxK

U2 - 10.1080/19420862.2020.1802187

DO - 10.1080/19420862.2020.1802187

M3 - Article

C2 - 32835602

AN - SCOPUS:85089740550

SN - 1942-0862

VL - 12

JO - mAbs

JF - mAbs

IS - 1

M1 - 1802187

ER -

Novel monoclonal antibodies to the SERINC5 HIV-1 restriction factor detect endogenous andvirion-associated SERINC5

Abstract

Keywords

Access to Document

Fingerprint

Cite this