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VISP: Center for Viral Infection Structural Proteomics

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VISP: Center for Viral Infection Structural Proteomics
SARS-CoV
Influenza virus
Herpesvirus
Flaviviruses
Poxviruses
  

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 About VISP

 

The Viral Infection Structural Proteomics (VISP) Center is working with the viral pathogen community to structurally characterize and understand critical virus and host proteins and their functional interactions using high throughput structural biology technologies and to provide the information rapidly back to the scientific community.

 Severe Acute Respiratory Syndrome Coronavirus

The goal of the Center for Functional and Structural Proteomics of SARS-CoV related proteins (FSPS)  is to provide a comprehensive characterized catalogue of all the SARS-CoV related proteins and associated functions at the viral and host levels to enable the development of therapeutic interventions. The Center for Functional and Structural Proteomics of SARS CoV related proteins (FSPS) is supported by NIH/NIAID as a Proteomics Resource Center through Contract #HHS266200400058C.

Influenza virus

The goal of this effort is to understand infectivity and specificity of the influenza virus and to determine structures of proteins (and/or their constituent domains) that are involved in viral replication and host response.

Human Herpesvirus 8 

The goal here is to study the structures of HHV8 proteins and their interactions with host ligands and to generate therapeutic targets and accelerate understanding of Kaposi's Sarcoma Herpesvirus biology and effective anti-viral and/or anti-tumor drug design.

Flaviviruses

The goal here is to determine the structures of flavivirus proteins, host proteins involved in viral replication and host proteins that modulate entry and the immune response. This knowledge would inform the biology of these viruses and also guide the development of vaccines and anti-virals.

Poxviruses

Poxviruses cause emerging infectious diseases and are potential bioterrorism agents. The goal is to determine the structures of poxvirus proteins that are involved in viral entry, assembly and replication, towards the development of prophylactics and therapeutics.

 Research Opportunities and Open Positions

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 VISP Kuhn Stevens Publications
Title Link Authors Journal Date
Proteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3   PubMed Entry   Neuman, B.W., Joseph, J.S., Saikatendu, K.S., Serrano, P., Chatterjee, A., Johnson, M.A., Liao, L., Klaus, J.P.,   Journal of Virology   3/16/2008  
International research networks in viral structural proteomics: Again, lessons from SARS.   Pubmed Entry   Canard, B., Joseph, J.S., Kuhn, P.   Antiviral Res   12/1/2007  
Crystal structure of a monomeric form of SARS-CoV endonuclease nsp15 suggests a role for hexamerization as an allosteric switch   Link   Joseph JS, et al.   Journal of Virology   2/27/2007  

 VISP Collaborator Publications
Human Cytomegaloviruses lacking UL128-150 cannot enter epithelial cells and have an additional defect in early stages of infecting endothelial cellsUse SHIFT+ENTER to open the menu (new window).
PMID: 16378974Ryckman M, et al.J. Virol.1/1/2006
Interferon regulatory factor 3 is necessary for induction of antiviral genes during human cytomegalovirus infection.Use SHIFT+ENTER to open the menu (new window).
PMID: 16379004DeFilippis VR, et al.J Virol.1/1/2006
Mapping the structure and function of the E1 and E2 glycoproteins in alphavirusesUse SHIFT+ENTER to open the menu (new window).
PMID: 16407066Mukhopadhyay S, et al.Structure1/1/2006
  		 
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 Member Laboratories
  Peter Kuhn and Ray Stevens labs at TSRI
The Kuhn and Stevens labs focus on understanding viruses and their host interactions through protein structure determination on a proteome-wide scale using advanced high-throughput structural genomics technologies, with a view to developing novel therapeutics and diagnostics.
  Mike Buchmeier lab at TSRI
Mike Buchmeier's lab is interested in the pathogenesis and control of emerging infections, the structure and function of viral glycoproteins, the mechanisms by which viruses interact with the host during persistent infection, and the way in which viruses contribute to a variety of autoimmune and neurodegenerative diseases.
  Ian Wilson lab at TSRI
A major goal of the Wilson lab is to employ X-ray crystallography to understand structure-function relationships and immunologic recognition of pathogens including viruses such as HIV-1, influenza virus and SARS-CoV.
  Kurt Wüthrich lab at TSRI
The Wüthrich lab develops and applies state-of-the-art NMR methods to study protein structure, function and folding. As part of structural genomics initiatives, this lab has solved NMR structures of several proteins, including membrane proteins and those of the SARS-CoV.
  Jay Nelson lab at OHSU
The long-term goal of Jay Nelson's laboratory is to understand the molecular basis of disease mediated by pathogenic human viruses.
  Richard Kuhn and Michael Rossmann at Purdue Univ.
Richard Kuhn's lab interests lie in the study of the molecular mechanisms involved in virus gene expression and the nature of virus-host interactions such as cell receptor binding, fusion, replication and assembly of several families of RNA containing viruses. Michael Rossmann's research interests are in virus structural biology.
  Ming Luo lab at UAB
Development of effective and economic therapy of infectious diseases requires thorough understanding of the biology of these infectious agents and innovative approaches to the problems. Ming Luo's laboratory has been involved in X-ray crystallographic analysis of critical proteins and design of novel drugs based on the protein structure.

 Interesting Links
  American Society for Microbiology
  Resource Center for Biodefense Proteomics Research