Yizhi Jane Tao | |
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Occupation(s) | Professor of Biochemistry and Cell Biology at Rice University, mapped atomic structure of the influenza A virus nucleoprotein trimer, named among the top ten most influential Chinese of 2006 by a consortium of China’s leading media outlets |
Yizhi Jane Tao is a Chinese biochemist, structural biologist, and professor of biochemistry and cell biology at Rice University in Houston, Texas. Professor Tao led a team of researchers to be the first to map the structure of the influenza A virus nucleoprotein to an atomic level, a feat which circulated widely in the popular press. [1] [2] She was named among the top ten most influential Chinese of 2006 by a consortium of China's leading media outlets including Phoenix Satellite Television, China News Service, Asia Newsweek, and World Journal. [3] [4]
All negative-sense RNA viruses encode a nucleoprotein that surrounds the virus and allows for replication. Tao discovered that the nucleoprotein for influenza A has a distinctive loop that is necessary for the viral genome to be organized into its double-helix hairpin structure. Tao then compared the amino acid sequences of different influenza viruses and found that the nucleoprotein loop she identified is conserved among influenza viruses. [5] [6] Since then, Tao has also solved the structure of a capsid protein coat for a double-stranded fungal RNA virus. [5] [7]
Born in China, Yizhi Jane Tao received a B.Sc. degree in biology from Peking University in Beijing, China in 1992. She later received her Ph.D. in biological sciences from Purdue University while studying bacteriophages under the German-American biophysicist Michael Rossmann, whose lab uncovered a 3D viral structure. [5] [8] She completed a postdoctoral fellowship under Stephen C. Harrison at Harvard University from 1999 to 2002, which also focused on uncovering virus structures. [5] [9] Upon completing her postdoctoral studies, Tao joined the faculty of Rice University, where she has made important contributions to the study of influenza, hepatitis, and birnaviruses. In 2018, Tao became a full professor at the university, and she currently leads The Tao Laboratory.
Research in the Tao Laboratory in the Department of BioSciences at Rice University focuses on RNA viruses. While RNA is known for being the intermediate between the genetic information in DNA and the proteins created from it, in RNA viruses, RNA contains the genetic information. Many RNA viruses can cause disease in humans, such as Hepatitis C, Ebola, HIV, and influenza. [10] RNA viruses can also infect bacterial and yeast hosts. RNA viruses are categorized into single- or double-stranded and plus or minus sense. RNA viruses work by reverse transcription, where DNA is created from RNA templates. [11] The reactions necessary for reverse transcription to occur are catalyzed by RNA-dependent RNA polymerases, a class of enzymes involved in replication and transcription. [12]
The Tao Lab uses electron microscopy, X-ray crystallography, and other biochemical and biophysical methods to understand the infection mechanism of RNA viruses. The lab hopes to help prevent and control viral disease by understanding the mechanism behind these viruses. [12]
Current projects in the Tao Lab are focused on Orsay virus, influenza viruses, picobirnavirus, ccFV-1, dinornavirus, and human astrovirus, some of which are described below. [12]
Astroviruses are small, single-stranded RNA viruses that can infect humans, birds, and other mammals. They are not surrounded by a viral envelope. Astroviruses have an icosahedral shape made of 20 identical equilateral triangular sides and are plus-sense, meaning the genetic information can be directly translated into proteins. Human astroviruses have a genome with approximately 7,000 bases. This genome encodes three important proteins: nonstructural proteins 1a and 1ab and the viral capsid protein (CP). The Tao Lab has determined the structure of the capsid protein core and surface spike. The lab also discovered that the capsid protein has a similar structure in astroviruses and the hepatitis E virus. The Tao Lab is currently investigating structural changes to the capsid protein that allows for the virus to infect a host cell even when treated with protease, which is used to slow the progression of other RNA virus infections. [12]
The Tao Lab is working to better understand the Orsay virus life cycle. Caenorhabditis elegans is a model organism in biology research. Orsay virus is the only type of virus known to infect C. elegans worms. Orsay infection in C. elegans is chronic and not lethal. Since C. elegans are frequently handled in the lab and can remain infected with Orsay virus for a long time, they are a convenient way to study Orsay virus. The positive sense, single-stranded Orsay genome encodes an RNA polymerase, a viral capsid protein (CP) and a nonstructural protein delta. Previous Tao Lab research has discovered that bound CP-delta proteins form a fiber that is part of the infectious virion. The CP-delta head fiber is involved in receptor binding and host entry, helping the virus infect its host cell. The delta protein on its own is involved in nonlytic viral egress. [12] [13]
Influenza viruses, also called the “flu” and known for the annual vaccine, are a serious public health concern. There are four types of influenza viruses: A, B, C, and D. Influenza D Virus (IDV) was first isolated in 2011. IDV infects cattle, pigs, and other ruminants. The Tao Lab aims to understand how the IDV nonstructural protein 1 (NS1) compares to the Influenza A Virus nonstructural protein 1. The lab also hopes to uncover the mechanism that creates IDV matrix proteins M1 and M2. Understanding the structure and function of NS1 and M1 proteins will help the lab understand IDV replication and pathogenesis. [12]
A capsid is the protein shell of a virus, enclosing its genetic material. It consists of several oligomeric (repeating) structural subunits made of protein called protomers. The observable 3-dimensional morphological subunits, which may or may not correspond to individual proteins, are called capsomeres. The proteins making up the capsid are called capsid proteins or viral coat proteins (VCP). The capsid and inner genome is called the nucleocapsid.
A DNA vaccine is a type of vaccine that transfects a specific antigen-coding DNA sequence into the cells of an organism as a mechanism to induce an immune response.
Wendell Meredith Stanley was an American biochemist, virologist and Nobel laureate.
Antigenic drift is a kind of genetic variation in viruses, arising from the accumulation of mutations in the virus genes that code for virus-surface proteins that host antibodies recognize. This results in a new strain of virus particles that is not effectively inhibited by the antibodies that prevented infection by previous strains. This makes it easier for the changed virus to spread throughout a partially immune population. Antigenic drift occurs in both influenza A and influenza B viruses.
Nucleoproteins are proteins conjugated with nucleic acids. Typical nucleoproteins include ribosomes, nucleosomes and viral nucleocapsid proteins.
The Matrix-2 (M2) protein is a proton-selective viroporin, integral in the viral envelope of the influenza A virus. The channel itself is a homotetramer, where the units are helices stabilized by two disulfide bonds, and is activated by low pH. The M2 protein is encoded on the seventh RNA segment together with the M1 protein. Proton conductance by the M2 protein in influenza A is essential for viral replication.
The M1 protein is a matrix protein of the influenza virus. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously.
Viral matrix proteins are structural proteins linking the viral envelope with the virus core. They play a crucial role in virus assembly, and interact with the RNP complex as well as with the viral membrane. They are found in many enveloped viruses including paramyxoviruses, orthomyxoviruses, herpesviruses, retroviruses, filoviruses and other groups.
Spanish flu research concerns studies regarding the causes and characteristics of the Spanish flu, a variety of influenza that in 1918 was responsible for the worst influenza pandemic in modern history. Many theories about the origins and progress of the Spanish flu persisted in the literature, but it was not until 2005, when various samples of lung tissue were recovered from American World War I soldiers and from an Inupiat woman buried in permafrost in a mass grave in Brevig Mission, Alaska, that significant genetic research was made possible.
Ian Andrew Wilson is the Hansen Professor of Structural Biology and chair of the Department of Integrative Structural and Computational Biology at the Scripps Research Institute in San Diego, California, United States.
A virus is a submicroscopic infectious agent that replicates only inside the living cells of an organism. Viruses infect all life forms, from animals and plants to microorganisms, including bacteria and archaea. Viruses are found in almost every ecosystem on Earth and are the most numerous type of biological entity. Since Dmitri Ivanovsky's 1892 article describing a non-bacterial pathogen infecting tobacco plants and the discovery of the tobacco mosaic virus by Martinus Beijerinck in 1898, more than 11,000 of the millions of virus species have been described in detail. The study of viruses is known as virology, a subspeciality of microbiology.
Bacteriophage Qbeta, commonly referred to as Qbeta or Qβ, is a species consisting of several strains of positive-strand RNA virus which infects bacteria that have F-pili, most commonly Escherichia coli. Its linear genome is packaged into an icosahedral capsid with a diameter of 28 nm. Bacteriophage Qβ enters its host cell after binding to the side of the F-pilus.
Jack Leonard Strominger is the Higgins Professor of Biochemistry at Harvard University, specializing in the structure and function of human histocompatibility proteins and their role in disease. He won the Albert Lasker Award for Basic Medical Research in 1995.
Importin alpha, or karyopherin alpha refers to a class of adaptor proteins that are involved in the import of proteins into the cell nucleus. They are a sub-family of karyopherin proteins.
Peter Palese is a United States microbiologist, researcher, inventor and the Horace W. Goldsmith Professor in the Department of Microbiology at the Icahn School of Medicine at Mount Sinai in New York City, and an expert in the field of RNA viruses.
Robert A. Lamb was a British-American virologist. He was the Kenneth F. Burgess Professor at Northwestern University and since 1991, an investigator of the Howard Hughes Medical Institute. From 1990 to 2016, he was the John Evans Professor of Molecular and Cellular Biology at Northwestern University.
The first step of transcription for some negative, single-stranded RNA viruses is cap snatching, in which the first 10 to 20 residues of a host cell RNA are removed (snatched) and used as the 5′ cap and primer to initiate the synthesis of the nascent viral mRNA. The viral RNA-dependent RNA polymerase (RdRp) can then proceed to replicate the negative-sense genome from the positive-sense template. Cap-snatching also explains why some viral mRNA have 5’ terminal extensions of 10-20 nucleotides that are not encoded for in the genome. Examples of viruses that engage in cap-snatching include influenza viruses (Orthomyxoviridae), Lassa virus (Arenaviridae), hantaan virus (Hantaviridae) and rift valley fever virus (Phenuiviridae). Most viruses snatch 15-20 nucleotides except for the families Arenaviridae and Nairoviridae and the genus Thogotovirus (Orthomyxoviridae) which use a shorter strand.
Jue Chen is a Chinese-born American structural biologist and biochemist. She is the William E. Ford professor of biochemistry and head of the Laboratory of Membrane Biology and Biophysics at the Rockefeller University and a Howard Hughes Medical Institute investigator. Her research focuses on elucidating the structure and function of ATP-binding cassette (ABC) transporters.
Mei Hong is a Chinese-American biophysical chemist and professor of chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.
Ervin Fodor is a British virologist of Hungarian origin born in Czechoslovakia. He is Professor of Virology holding the position of reader in experimental pathology in the Sir William Dunn School of Pathology at the University of Oxford. He is also a professorial fellow at Exeter College, Oxford.