Tina M Cairns

Summary

Affiliation: University of Pennsylvania
Country: USA

Publications

  1. pmc Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
    J Virol 80:2596-608. 2006
  2. pmc Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    Doina Atanasiu
    Department of Microbiology, School of Dental Medicine, and Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104
    Proc Natl Acad Sci U S A 104:18718-23. 2007
  3. pmc Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimeras
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
    J Virol 77:6731-42. 2003
  4. ncbi request reprint Contribution of cysteine residues to the structure and function of herpes simplex virus gH/gL
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    Virology 332:550-62. 2005
  5. pmc Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment
    Tina M Cairns
    Department of Microbiology, University of Pennsylvania, 4010 Locust St, Levy Rm 233, Philadelphia, PA 19104, USA
    J Virol 85:6175-84. 2011
  6. pmc N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    J Virol 81:5102-11. 2007
  7. pmc Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    Brian P Hannah
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    J Virol 83:6825-36. 2009
  8. pmc Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA
    J Virol 88:2677-89. 2014
  9. pmc Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization
    Eric Lazear
    Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
    J Virol 86:1563-76. 2012
  10. pmc Herpes virus fusion and entry: a story with many characters
    Roselyn J Eisenberg
    Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    Viruses 4:800-32. 2012

Detail Information

Publications14

  1. pmc Epitope mapping of herpes simplex virus type 2 gH/gL defines distinct antigenic sites, including some associated with biological function
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
    J Virol 80:2596-608. 2006
    ..Several recognize important functional domains of gH2, gL2, or the complex. We suggest a common grouping scheme for all of the known MAbs against gH/gL of both HSV-1 and HSV-2...
  2. pmc Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    Doina Atanasiu
    Department of Microbiology, School of Dental Medicine, and Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104
    Proc Natl Acad Sci U S A 104:18718-23. 2007
    ..Thus, when gD binds its receptor, the core fusion machinery is triggered to form a multiprotein complex as a step in fusion and possibly virus entry...
  3. pmc Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimeras
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
    J Virol 77:6731-42. 2003
    ..However, these chimeras functioned poorly in gD-null virus complementation assays. The results highlight the fact that these two functional assays are measuring two related but distinct processes...
  4. ncbi request reprint Contribution of cysteine residues to the structure and function of herpes simplex virus gH/gL
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    Virology 332:550-62. 2005
    ..These findings suggest that there is a structural difference in the gH2 N-terminus as compared to gH1. We also present genetic evidence for at least one disulfide bond within gH2, between cysteines 2 and 4...
  5. pmc Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment
    Tina M Cairns
    Department of Microbiology, University of Pennsylvania, 4010 Locust St, Levy Rm 233, Philadelphia, PA 19104, USA
    J Virol 85:6175-84. 2011
    ..Our liposome data support the concept that low pH triggers conformational changes to both proteins that allow gH/gL to physically interact with gB...
  6. pmc N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    J Virol 81:5102-11. 2007
    ..Additional mutagenesis identified L66 and L72 as important for function. Together, our results highlight several key gH residues: R39, Y41, W42, and D44 for gH transport and L66 and L72 for gH/gL structure and function...
  7. pmc Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops
    Brian P Hannah
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    J Virol 83:6825-36. 2009
    ..Taken together, our data suggest that gB associates with lipid membranes via a fusion domain of key hydrophobic and hydrophilic residues and that this domain associates with lipid membranes during fusion...
  8. pmc Mechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B
    Tina M Cairns
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA
    J Virol 88:2677-89. 2014
    ..We also generated a peptide antibody against one of the gB fusion loops; its properties provide insight into the way the fusion loops function as gB transits from its prefusion form to an active fusogen...
  9. pmc Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization
    Eric Lazear
    Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, USA
    J Virol 86:1563-76. 2012
    ..We suggest that MC2 and MC5 prevent gD from performing a function that triggers later steps leading to fusion and that the epitope for MC2 is normally occluded by the C-term of the gD ectodomain...
  10. pmc Herpes virus fusion and entry: a story with many characters
    Roselyn J Eisenberg
    Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA
    Viruses 4:800-32. 2012
    ..Our model highlights what is known and also provides a framework to address mechanistic questions about fusion by HSV and herpesviruses in general...
  11. ncbi request reprint Repertoire of epitopes recognized by serum IgG from humans vaccinated with herpes simplex virus 2 glycoprotein d
    J Charles Whitbeck
    Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA
    J Virol 88:7786-95. 2014
    ..This suggests that optimal virus-neutralizing activity is achieved by strong and balanced responses to the four major discontinuous neutralizing epitopes of gD2...
  12. pmc Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry
    Eric Lazear
    Department of Microbiology, University of Pennsylvania, 240 S 40th St, Levy Rm 233, Philadelphia, PA 19104, USA
    J Virol 82:700-9. 2008
    ..Based upon the properties of the panel of mutants we conclude that fusion requires greater flexibility of the gD ectodomain C terminus than does receptor binding...
  13. doi request reprint HCMV grabs a mechanism to escape neutralization
    Roselyn J Eisenberg
    School of Veterinary Medicine, University of Pennsylvania, Philadelphia, USA
    Cell Host Microbe 10:177-8. 2011
    ..2011) found that MSL-109 rapidly induces antibody resistance by a nongenetic mechanism. Their results shed light on how antibodies can interact with their targets both outside and inside infected cells and virions...
  14. pmc Overlapping roles of the Rous sarcoma virus Gag p10 domain in nuclear export and virion core morphology
    Lisa Z Scheifele
    Department of Medicine, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA
    J Virol 81:10718-28. 2007
    ..Together, these results indicate that the p10 NES domain of Gag is critical for virus replication and that it plays overlapping roles required for the nuclear shuttling of Gag and for the maintenance of proper virion core morphology...