Wesley I. Sundquist | |
---|---|
Born | September 11, 1959 (age 65) |
Alma mater | Carleton College (BA; 1981) Massachusetts Institute of Technology (PhD; 1988) |
Known for | Research in HIV assembly and membrane remodeling |
Spouse | Nola Sundquist |
Children | 2 |
Awards | Louisa Gross Horwitz Prize (2024) [1] |
Scientific career | |
Fields | Structural biology, biochemistry, virology, cell biology |
Institutions | University of Utah (1992) MRC Laboratory of Molecular Biology |
Wesley I. Sundquist is an American biochemist. Sundquist is Samuels Chair, Distinguished Professor, and Chair of the University of Utah Department of Biochemistry. [2] Sundquist's research focuses on cellular, molecular and structural biology of retroviruses, particularly Human Immunodeficiency Virus (HIV), and on cellular membrane remodeling by the Endosomal Sorting Complexes Required for Transport (ESCRT) pathway.
Sundquist was born in Saint Paul, Minnesota on September 11, 1959. He grew up in Saint Paul and Washington, D.C. He received his bachelor's degree in chemistry from Carleton College in Minnesota in 1981. Sundquist completed a PhD in chemistry at the Massachusetts Institute of Technology with Stephen J. Lippard in 1988. He was then a postdoctoral fellow at the MRC Laboratory of Molecular Biology in Cambridge, England with Sir Aaron Klug. In 1992, Sundquist joined the University of Utah Department of Biochemistry.
The HIV capsid encloses the viral RNA genome and facilitates viral replication. Sundquist and colleagues defined the unusual fullerene cone architecture of the viral capsid [3] [4] and identified essential functions of the capsid in HIV-1 replication, [5] which helped enable development of the potent and long-lasting Lenacapavir capsid inhibitor by Gilead Sciences. The Sundquist lab also reconstituted capsid-dependent HIV reverse transcription and integration in a cell-free system. [6]
To spread infection, viruses must shed from infected cells. Sundquist and colleagues found that retroviruses like HIV exit cells using the host ESCRT pathway. [7] [8] They also used this information to design new proteins that can assemble into nanocages, exit producer cells, and carry cargoes into new target cells. [9]
Cytokinesis separates one replicating cell into two daughter cells. Sundquist's lab studies this process by determining the structures and functions of factors that function to complete and regulate cytokinesis. [10] [11] [12]
Sundquist met his wife Nola in 1983 when they were graduate students at MIT, and they were married in 1987. As of 2024, their son Christopher is a Corporate and Securities Attorney at the Gunderson Detmer Law Firm in Boston [18] and their daughter Emily is a fourth-year medical student at Harvard Medical School.
The term viral protein refers to both the products of the genome of a virus and any host proteins incorporated into the viral particle. Viral proteins are grouped according to their functions, and groups of viral proteins include structural proteins, nonstructural proteins, regulatory proteins, and accessory proteins. Viruses are non-living and do not have the means to reproduce on their own, instead depending on their host cell's machinery to do this. Thus, viruses do not code for most of the proteins required for their replication and the translation of their mRNA into viral proteins, but use proteins encoded by the host cell for this purpose.
Group-specific antigen, or gag, is the polyprotein that contains the core structural proteins of an Ortervirus. It was named as such because scientists used to believe it was antigenic. Now it is known that it makes up the inner shell, not the envelope exposed outside. It makes up all the structural units of viral conformation and provides supportive framework for mature virion.
Tumor susceptibility gene 101, also known as TSG101, is a human gene that encodes for a cellular protein of the same name.
Programmed cell death 6-interacting protein also known as ALIX is a protein that in humans is encoded by the PDCD6IP gene.
Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.
Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.
Vacuolar protein sorting-associated protein 4B is a protein that in humans is encoded by the VPS4B gene.
Vacuolar protein sorting-associated protein 28 homolog is a protein that in humans is encoded by the VPS28 gene.
Charged multivesicular body protein 4b is a protein that in humans is encoded by the CHMP4B gene.
Charged multivesicular body protein 4a is a protein that in humans is encoded by the CHMP4A gene.
Charged multivesicular body protein 5 is a protein that in humans is encoded by the CHMP5 gene.
Charged multivesicular body protein 6 is a protein that in humans is encoded by the CHMP6 gene. It is one of charged multivesicular body proteins and a part of endosomal sorting complexes required for transport-III (ESCRT-III) complex.
Vacuolar-sorting protein SNF8 is a protein that in humans is encoded by the SNF8 gene. It is a part of ESCRT-II complex.
Charged multivesicular body protein 4c is a protein that in humans is encoded by the CHMP4C gene.
The p24 capsid protein is the most abundant HIV protein with each virus containing approximately 1,500 to 3,000 p24 molecules. It is the major structural protein within the capsid, and it is involved in maintaining the structural integrity of the virus and facilitating various stages of the viral life cycle, including viral entry into host cells and the release of new virus particles. Detection of p24 protein's antigen can be used to identify the presence of HIV in a person's blood and diagnose HIV/AIDS, however, more modern tests have taken their place. After approximately 50 days of infection, the p24 antigen is often cleared from the bloodstream entirely.
The endosomal sorting complexes required for transport (ESCRT) machinery is made up of cytosolic protein complexes, known as ESCRT-0, ESCRT-I, ESCRT-II, and ESCRT-III. Together with a number of accessory proteins, these ESCRT complexes enable a unique mode of membrane remodeling that results in membranes bending/budding away from the cytoplasm. These ESCRT components have been isolated and studied in a number of organisms including yeast and humans. A eukaryotic signature protein, the machinery is found in all eukaryotes and some archaea.
Scott D. Emr is an American cell biologist and the founding and current Director of the Weill Institute for Cell and Molecular Biology at Cornell University, where he is also a Frank H.T. Rhodes Class of 1956 Professor at the Department of Molecular Biology and Genetics.
Vacuolar protein sorting 37 homolog A is a protein in humans that is encoded by the VPS37A gene. It is a member of the endosomal sorting complex required for transport (ESCRT) system.
In the management of HIV/AIDS, HIV capsid inhibitors are antiretroviral medicines that target the capsid shell of the virus. This is in contrast to most current antiretroviral drugs used to treat HIV, which do not directly target the viral capsid. These have also been termed "Capsid-targeting Antivirals", "Capsid Effectors", and "Capsid Assembly Modulators (CAMs)". Because of this, drugs that specifically inhibit the HIV capsid are being developed in order to reduce the replication of HIV, and treat infections that have become resistant to current antiretroviral therapies.
Carol A. Carter is an American microbiologist. She is Distinguished Professor in the Department of Microbiology and Immunology of the Renaissance School of Medicine at Stony Brook University, and member of the National Academy of Sciences.