Ronald C. Montelaro, PhD

Ronald Montelaro Co-Director, CVR

Microbiology & Molecular Genetics
9016 BST3
3501 Fifth Avenue
Pittsburgh, Pennsylvania 15261

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Phone: (412) 648-8869
Fax: (412) 624-4440
Lab Information

Phone: (412) 648-8874
Fax: (412) 624-4440
Lab Members:
      • Deslouches, Berthony
      • Hasek, Mary Louise
      • Montelaro, Ronald C
      • Steckbeck, Jonathan Damien
      • Sturgeon, Timothy J


      Dr. Montelaro is a Professor in the Department of Microbiology and Molecular Genetics of the University of Pittsburgh School of Medicine with secondary appointments in the Department of Infectious Diseases and Immunology (Graduate School or Public Health) and the Department of Medicine Division of Infectious Diseases. He serves as the Co-Director of the Center for Vaccine Research and the Director of the Peptide Synthesis Core. He received his PhD in Biochemistry in 1975 from the University of Wisconsin-Madison. His research interest is in viral immunology and vaccine development, especially as related to AIDS, emerging diseases, and biodefense.


      The primary focus of the Montelaro lab is to elucidate the intricate interactions between viral pathogens and host immune responses to determine the mechanisms by with host immunity contributes to protection and disease and to serve as a basis for the development of effective vaccines. A particular interest of the lab is to develop effective strategies to overcome the challenge of natural viral antigenic variation that has evolved as a common complication to the development of effective vaccines to important viral diseases, including those related to biodefense and emerging infectious diseases. Systems currently under investigation include HIV-1 and related animal lentiviruses (SHIV, SIV, and EIAV). Studies in these systems include investigation of the nature and role of antigenic variation during infection, the development of novel assays to characterize virus-specific innate, humoral, and cellular immune responses, and the design of engineered immunogens for effective vaccination against variant strains of a particular virus. In addition to these vaccine related studies, the lab also maintains a research program to develop novel de novo antimicrobial peptides (engineered cationic amphipathic peptides, or eCAPs) that can be used to inactivate a diverse spectrum of bacteria or enveloped viruses in a prophylactic or therapeutic treatment modalities.

Selected Publications

  • Steckbeck, J., Sun, C., Sturgeon, T., and Montelaro, R. (2013) Detailed topology mapping reveals substantial exposure of the “cytoplasmic” C-terminal tail (CTT) sequences in the HIV-1 Env protein at the cell surface. PLoS One 8(5):e65220

  • Paranjape, S., Lauer, T., Montelaro, R., and Mietzner, T. (2013) Modulation of proinflammatory activity by the engineered cationic antimicrobial peptide WLBU-2. F1000Research 2:36 (doi:10.34 10/f1000research.2-36.v1)

  • Deslouches, B., Steckbeck, J., Craigo, J., Doi, Y., Mietzner, T., and Montelaro, R. (2013) Rational design of engineered antimicrobial peptides consisting exclusively of arginine and tryptophan: WR eCAP activity against multi-drug resistant pathogens. Antimicrobial Agents and Chemotherapy 57: 2511-2521.

  • Craigo, J., Ezzelarab, C., Cook, S., Chong, L., Horohov, D., Issel, C., and Montelaro, R. (2013) Envelope determinants of equine lentiviral vaccine protection. PLoS One 8(6):e66093.

  • Boscia, A., Akabori, K., Benamram, Z., Michel, J., Jablin, M., Steckbeck, J., Montelaro, R., Nagle, J., and Tristram-Nagle, S. (2013) Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein. Biophysical J. 105: 657-666.

  • Yang, Y. Kulka, K., Montelaro, R., Reinhart, T., Sisson, J., Aderem, A., and Ojha, A. (2014) A hydrolase of trehalose dimycolate induces nutrient influx and stress sensitivity to balance intracellular growth of Mycobacterium tuberculosis. Cell Host & Microbe 15: 153-163.

  • Kuhlmann, A., Steckbeck, J., Sturgeon, T., Craigo, J., and Montelaro, R. (2014) Unique functional properties of conserved arginine residues in the lentivirus lytic peptide domains of the C-terminal tail of HIV-1 gp41. J. Biol. Chem. 289: 7630-7640.

  • Steckbeck, J., Deslouches, B., and Montlelaro, R. (2013) Antimicrobial peptides: New drugs for bad bugs? Exp. Opinion Biol. Therap. 14: 10.1517/14712598.2013.844227

  • Craigo, J. and Montelaro, R. (2013) Lessons in AIDS vaccine development learned from studies of equine infectious anemia virus infection and disease. Viruses 5: 2963-2976.

  • Steckbeck, J., Kuhlmann, AS, and Montelaro, R. (2014) Structural and functional comparisons of retroviral envelope protein C-terminal domain: still much to learn. Viruses 6: 284-300. PMC3917443

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Last Modified: Tuesday, July 16, 2013 at 12:15:38 PM
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