Results 11 to 20 of about 370 (99)

SERINC Proteins Potentiate Antiviral Type I IFN Induction and Proinflammatory Signaling Pathways

Proceedings, 2020
T cell SERINC proteins were recently identified as human immunodeficiency virus (HIV) restriction factors that diminish viral infectivity by incorporation into virions.
Cong Zeng, Abdul A. Waheed, Tianliang Li, Jingyou Yu, Yi-Min Zheng, Jacob Yount, Haitao Wen, Eric O. Freed, Shan-Lu Liu   +8 more
doaj   +3 more sources

Nef Obtained from Individuals with HIV-1 Vary in Their Ability to Antagonize SERINC3- and SERINC5-Mediated HIV-1 Restriction

Viruses, 2021
Nef is a multifunctional viral protein that has the ability to downregulate cell surface molecules, including CD4 and major histocompatibility complex class I (MHC-I) and, as recently shown, also members of the serine incorporator family (SERINC).
Zita Kruize, Ad C. van Nuenen, Stan W. van Wijk, Arginell F. Girigorie, Karel A. van Dort, Thijs Booiman, Neeltje A. Kootstra   +6 more
doaj   +2 more sources

A bipartite structural organization defines the SERINC family of HIV-1 restriction factors [PDF]

Nature Structural and Molecular Biology, 2020
The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of human SERINC5 and its orthologue from Drosophila ...
C V Robinson, Phillip J Stansfeld, Giada Mattiuzzo   +2 more
exaly   +6 more sources

SERINC5 Potently Restricts Retrovirus Infection In Vivo

mBio, 2020
The serine incorporator (SERINC) proteins are multipass transmembrane proteins that affect sphingolipid and phosphatidylserine synthesis. Human SERINC5 and SERINC3 were recently shown to possess antiretroviral activity for a number of retroviruses ...
Uddhav Timilsina, Supawadee Umthong, Brian Lynch, Aimee Stablewski, Spyridon Stavrou   +4 more
doaj   +2 more sources

Potent Enhancement of HIV-1 Replication by Nef in the Absence of SERINC3 and SERINC5

mBio, 2019
It has recently emerged that HIV-1 Nef counteracts the antiviral host proteins SERINC3 and SERINC5. In particular, SERINC5 inhibits the infectivity of progeny virions when incorporated.
Yuanfei Wu, Balaji Olety, Eric R. Weiss, Elena Popova, Hikaru Yamanaka, Heinrich Göttlinger   +5 more
doaj   +3 more sources

SERINC5 Is an Unconventional HIV Restriction Factor That Is Upregulated during Myeloid Cell Differentiation

Journal of Innate Immunity, 2020
Classical antiviral restriction factors promote cellular immunity by their ability to interfere with virus replication and induction of their expression by proinflammatory cytokines such as interferons.
Ariane Zutz, Christian Schölz, Stephanie Schneider, Virginia Pierini, Maximilian Münchhoff, Kathrin Sutter, Georg Wittmann, Ulf Dittmer, Rika Draenert, Johannes R. Bogner, Oliver T. Fackler, Oliver T. Keppler   +11 more
doaj   +2 more sources

SERINC5-Mediated Restriction of HIV-1 Infectivity Correlates with Resistance to Cholesterol Extraction but Not with Lipid Order of Viral Membrane

Viruses, 2022
Serine incorporator 5 (SER5) is a protein that upon incorporation into virions inhibits HIV-1 infectivity by interfering with the ability of the Env glycoprotein to promote viral fusion.
Gregory B Melikyan, Yen-Cheng Chen, Mariana Marin   +2 more
exaly   +3 more sources

A Long Cytoplasmic Loop Governs the Sensitivity of the Anti-viral Host Protein SERINC5 to HIV-1 Nef

Cell Reports, 2018
We recently identified the multipass transmembrane protein SERINC5 as an antiviral protein that can potently inhibit HIV-1 infectivity and is counteracted by HIV-1 Nef.
Weiwei Dai, Yoshiko Usami, Yuanfei Wu, Heinrich Göttlinger   +3 more
doaj   +2 more sources

Disruption of Transmembrane Phosphatidylserine Asymmetry by HIV-1 Incorporated SERINC5 Is Not Responsible for Virus Restriction [PDF]

Biomolecules
Host restriction factor SERINC5 (SER5) incorporates into the HIV-1 membrane and inhibits infectivity by a poorly understood mechanism. Recently, SER5 was found to exhibit scramblase-like activity leading to the externalization of phosphatidylserine (PS ...
Gokul Raghunath, Elizabeth H. Abbott, Mariana Marin, Hui Wu, Judith Mary Reyes Ballista, Melinda A. Brindley, Gregory B. Melikyan   +6 more
doaj   +2 more sources

Serinc5 Regulates Sequential Chondrocyte Differentiation by Inhibiting Sox9 Function in Pre-Hypertrophic Chondrocytes. [PDF]

J Cell Physiol
ABSTRACT The growth plate is the primary site of longitudinal bone growth with chondrocytes playing a pivotal role in endochondral bone development. Chondrocytes undergo a series of differentiation steps, resulting in the formation of a unique hierarchical columnar structure comprising round, proliferating, pre‐hypertrophic, and hypertrophic ...
Hata K, Wakamori K, Hirakawa-Yamamura A, Ichiyama-Kobayashi S, Yamaguchi M, Okuzaki D, Takahata Y, Murakami T, Uzawa N, Yamashiro T, Nishimura R.   +10 more
europepmc   +2 more sources