Patricia G. Spear | |
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Born | Patricia Gail Spear 1942 (age 80–81) |
Alma mater | Florida State University, BA, 1964 Florida State University, MS, 1965 University of Chicago, PhD, 1969 |
Known for | Expertise in herpes simplex virus |
Spouse | Peter Meyer (d. 2002) |
Awards | National Academy of Sciences Member |
Scientific career | |
Institutions | Northwestern University |
Doctoral advisor | Bernard Roizman |
Patricia Gail Spear (born 1942) is an American virologist. She is a professor emeritus of microbiology and immunology at Northwestern University in Evanston, Illinois. She is best known for her pioneering work studying the herpes simplex virus. Spear is a past president of the American Society for Virology and an elected member of the National Academy of Sciences.
Spear began her undergraduate education at Florida State University. She went to study nursing and ultimately switched her major to bacteriology with a minor in chemistry and graduated in 1964. [1] One year later, she received her Master of Science from Florida State in bacteriology and then enrolled in a graduate program in virology at the University of Chicago.
For her doctoral work, Spear joined the laboratory of Bernard Roizman to conduct research on herpes simplex virus (HSV). In an interview, she noted: "I thought it was mind-blowing how the virus could change the shape and behavior of the cell before killing it off." [1] There, she developed a method to purify the herpes simplex enveloped nucleocapsid, known as a virion, and determined the number of proteins it contained using electrophoresis. [2] Following her PhD, she stayed in Roizman's laboratory for another two years, characterizing the approximately 30 HSV proteins she had identified.
In 1971, Spear became a postdoctoral fellow in the laboratory of Gerald Edelman at the Rockefeller University in New York City. There, she received intensive training in immunology, studying the development of the immune system in mice, tracking when the spleen and thymus become populated with T cells and B cells. [3] [4]
Following her postdoctoral fellowship, she became an assistant professor in the department of microbiology at the University of Chicago, focusing her research program on HSV, and then became chair of the department of microbiology and immunology at Northwestern University. [1]
During her tenure at the University of Chicago, Spear developed a new area of research studying HSV glycoproteins in the viral envelop. [1] Her group worked to describe the surface glycoproteins and characterized their functions in cell fusion and the immune response. In some mutant strains of HSV, infection promotes the fusion of infected host cells within lesions and is one possible mechanism by which the virus spreads from cell to cell. By studying different mutant strains of HSV, Spear found that the viral glycoprotein gB promotes cell fusion, while another glycoprotein called gC can act to suppress cell fusion. [5]
Spear has also investigated how HSV enters the host cell by working to identify cell-surface receptors recognized by the virus. Her group found that the initial cell-surface receptor for both HSV 1 and HSV2 is heparan sulfate, a carbohydrate component of some proteoglycans, and are recognized and bound by the viral glycoproteins gB and gC. [6] [7] When Spear re-located her laboratory from University of Chicago to Northwestern University, her team identified three different classes of entry receptor: a cell-surface protein called herpes virus entry mediator (HVEM), two members of the immunoglobulin superfamily called Nectin-1 and Nectin-2, and [8]
For 16 years, Spear served as chair of the department of microbiology and immunology at Northwestern University. From 2003 to 2004, she served as president of the American Society for Virology. [9]
Measles morbillivirus(MeV), also called measles virus (MV), is a single-stranded, negative-sense, enveloped, non-segmented RNA virus of the genus Morbillivirus within the family Paramyxoviridae. It is the cause of measles. Humans are the natural hosts of the virus; no animal reservoirs are known to exist.
Herpesviridae is a large family of DNA viruses that cause infections and certain diseases in animals, including humans. The members of this family are also known as herpesviruses. The family name is derived from the Greek word ἕρπειν, referring to spreading cutaneous lesions, usually involving blisters, seen in flares of herpes simplex 1, herpes simplex 2 and herpes zoster (shingles). In 1971, the International Committee on the Taxonomy of Viruses (ICTV) established Herpesvirus as a genus with 23 viruses among four groups. As of 2020, 115 species are recognized, all but one of which are in one of the three subfamilies. Herpesviruses can cause both latent and lytic infections.
Human Herpes Virus (HHV) Infected Cell Polypeptide 0 (ICP0) is a protein, encoded by the DNA of herpes viruses. It is produced by herpes viruses during the earliest stage of infection, when the virus has recently entered the host cell; this stage is known as the immediate-early or α ("alpha") phase of viral gene expression. During these early stages of infection, ICP0 protein is synthesized and transported to the nucleus of the infected host cell. Here, ICP0 promotes transcription from viral genes, disrupts structures in the nucleus known as nuclear dots or promyelocytic leukemia (PML) nuclear bodies, and alters the expression of host and viral genes in combination with a neuron specific protein. At later stages of cellular infection, ICP0 relocates to the cell cytoplasm to be incorporated into new virion particles.
Herpes simplex virus1 and 2, also known by their taxonomic names Human alphaherpesvirus 1 and Human alphaherpesvirus 2, are two members of the human Herpesviridae family, a set of viruses that produce viral infections in the majority of humans. Both HSV-1 and HSV-2 are very common and contagious. They can be spread when an infected person begins shedding the virus.
HHV Capsid Portal Protein, or HSV-1 UL-6 protein, is the protein which forms a cylindrical portal in the capsid of Herpes simplex virus (HSV-1). The protein is commonly referred to as the HSV-1 UL-6 protein because it is the transcription product of Herpes gene UL-6.
Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).
Anthony (Tony) Charles Minson, PhD, FMedSci is a British virologist known for his work on the biology of herpesviruses, and a university administrator. He was the Senior Pro-Vice-Chancellor of the University of Cambridge from 2003 to 2009. He is emeritus professor of virology at the university's Department of Pathology and an emeritus fellow of Wolfson College.
2F5 is a broadly neutralizing human monoclonal antibody (mAb) that has been shown to bind to and neutralize HIV-1 in vitro, making it a potential candidate for use in vaccine synthesis. 2F5 recognizes an epitope in the membrane-proximal external region (MPER) of HIV-1 gp41. 2F5 then binds to this epitope and its constant region interacts with the viral lipid membrane, which neutralizes the virus.
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Deepak Shukla is an American molecular virologist with expertise in herpesviruses. He contributed to the discovery of HSV-1 entry receptors and establishing a link between the receptors and HSV-1 induced ocular diseases such as keratitis and retinitis. He has authored over 100 published papers and several book chapters on herpes viruses.
Herpesvirus glycoprotein B is a viral glycoprotein that is involved in the viral cell entry of Herpes simplex virus (HSV). Herpesviruses have a lipid bilayer, called the envelope, which contains twelve surface glycoproteins. For infectivity to be attained, the double stranded DNA genome of HSV must enter the host cell through means of fusion of its envelope with the cellular membrane or via endocytosis. Other viral glycoproteins involved in the process of viral cell entry include gC, gB, gD, gH, and gL, but only gC, gB, gD, and gH are required for the fusion of the HSV's envelope with the cellular membrane. It can be noted that all herpesviruses have glycoproteins gB, gH, and gL.
David Mahan Knipe is the Higgins Professor of Microbiology and Molecular Genetics in the Department of Microbiology at the Harvard Medical School in Boston, Massachusetts and co-chief editor of the reference book Fields Virology. He returned to the Chair of the Program in Virology at Harvard Medical School in 2019, having previously held the position from 2004 through 2016 and served as interim Co-Chair of the Microbiology and Immunobiology Department from 2016 through 2018.
Almyra Oveta Fuller was an associate professor of microbiology and immunology at University of Michigan Medical School. She served as the director of the African Studies Center (ASC), faculty in the ASC STEM Initiative at the University of Michigan (U-M) and an adjunct professor at Payne Theological Seminary. Fuller was a virologist and specialized in research of Herpes simplex virus, as well as HIV/AIDS. Fuller and her research team discovered a B5 receptor, advancing the understanding of Herpes simplex virus and the cells it attacks.
Roselyn J. Eisenberg is a professor at The University of Pennsylvania and a member of the University's School of Veterinary Medicine and School of Dental Medicine. The majority of Eisenberg's research is focused on the herpes simplex virus and the poxvirus and how they enter into susceptible cells. She also studies glycoproteins, vaccines, virology and microbiology.
Joel D. Baines is an American virologist who is serving as dean of the School of Veterinary Medicine, Louisiana State University (LSU) since 2014.
Gabriella Campadelli-Fiume is a virologist with a primary research focus on herpes simplex virus, fusion and viral entry. She is a retired professor of virology from the University of Bologna, Italy.
Human herpes viruses, also known as HHVs, are part of a family of DNA viruses that cause several diseases in humans. One of the most notable functions of this virus family is their ability to enter a latent phase and lay dormant within animals for extended periods of time. The mechanism that controls this is very complex because expression of viral proteins during latency is decreased a great deal, meaning that the virus must have transcription of its genes repressed. There are many factors and mechanisms that control this process and epigenetics is one way this is accomplished. Epigenetics refers to persistent changes in expression patterns that are not caused by changes to the DNA sequence. This happens through mechanisms such as methylation and acetylation of histones, DNA methylation, and non-coding RNAs (ncRNA). Altering the acetylation of histones creates changes in expression by changing the binding affinity of histones to DNA, making it harder or easier for transcription machinery to access the DNA. Methyl and acetyl groups can also act as binding sites for transcription factors and enzymes that further modify histones or alter the DNA itself.
Pneumoviridae is a family of negative-strand RNA viruses in the order Mononegavirales. Humans, cattle, and rodents serve as natural hosts. Respiratory tract infections are associated with member viruses such as human respiratory syncytial virus. There are five species in the family which are divided between the genera Metapneumovirus and Orthopneumovirus. The family used to be considered as a sub-family of Paramyxoviridae, but has been reclassified as of 2016.
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