NAME
Robert Villafañe
TITLE
Associate Professor of Biochemistry
UC Berkeley
NYU School of Medicine
Massachusetts Institute of Technology (MIT)
MA
PhD
Post-Doc
1976
1985
1985-1989
Molecular Biology
Microbiology
Molecular Genetics
1985-1989
1989-1996
1996-2001
2001-present
Assistant Professor, Department of Microbiology, University of Tennessee-Knoxville
Associate Professor, UCC School of Medicine Department of Microbiology and Immunology
Bayamon, PR
Associate Professor, Department of Biochemistry, Ponce School of Medicine, Ponce, Puerto Rico
April 1990
1990,1993
New York University Honors Biology
Sackler Biomedical Fellow, NIH Trainee
Sigma Xi, Full Member
Visiting Prof, Carnegie Mellon Univ. April
Univ. of Tenn. Faculty Research Awards
Villafañe R, King J. J. Mol. Biol. 1988; 204: 607-619. The nature and distribution of temperature sensitive folding mutations in the tailspike gene ofbacteriophage P22.
King J, Fane B, Haase-Pettingell C, Mitraki A, Villafañe R, Yu M-H. In "Protein Folding: Deciphering the second half of the genetic code. (Ed. Lila Gierasch and Jonathan King), AAAS Symposia Series 1989; pp. 225-240. Identification of amino acid sequences influencing intracellular folding pathways using temperature-sensitive folding mutations.
King J, Fane B, Haase-Pettingell C, Mitraki A, Villafañe R. hi "Protein Design and the Development oj New Therapeutics and Vaccines." 1990 (Eds. J. B. Hook & George Poste) Smith Kline and Frencr Symposium, Plenum Press, pp. 59-78. Genetic analysis of polypeptide chain folding and misfolding ir vivo.
Bazinet C, Villafañe R, King J. J. Mol. Biol. 1990; 216:701-716. Novel second-site suppression of a cold- sensitive defect in phage P22 procapsid assembly.
Fane B, Villafañe R, Mitraki A, King J. J Biol. Chem. 1991; 261: 11640-11648. Identification of Globa Suppressors for Temperature-sensitive Folding Mutations of the P22 tailspike Protein.
Villafañe R, Fleming A, Haase-Pettingell C. J. Bacteriol. 1994; T76:T37-T42. Direct solatio'n of suppressors of temperature sensitive folding mutations.
Villafañe R, Black J. Arch Virol. 1994; 135: 179-183. Identification of four genes involved in the lysogenic pathway of the Salmonella newington bacterial virus e34.
Greenberg M, Dunlap J, Villafañe R J. Struct. Biol. 1995; 115:283-289. Identification of the tailspike protein from the Salmonella newington phage e34 and partial characterization of its phage-associated properties.
Villafañe R and Baksi K. PR Health Sci J 1999; 18:105-115. A tail of protein folding.
Kowalcyzk R J, Liberatore K, Villafañe R. PR Health Sci J 1999; 18:363-367. Suppressor mutations derived from the most severe protein folding mutation known.
Venza C, Vasquez A, Villafañe R. (2002) submitted to Microbiology. Defining sites on the P22 phage tailspike protein which affect its binding to the Salmonella typhimurium surface.
Salgado C, Otero M, Villafañe R. (2003) in preparation for Arch Virol. Extensive homology between two Salmonella phages: Salmonell typhimurium phage P22 and Salmonella newington phage ee .
Salgado C, Col6n J, Romero M, Venza C, Villafañe R. (2003) submitted to J. Biol. Chem. The tailspike protein from Salmonella typhimurium phage P22 may be a module for other Salmonella phage tail proteins.
G12RR03035 Villafane (PI) 9/1/98-8/31/03
NIH/GMS/RCMI Pilot Project
Conservation of ammo acids in an LPS binding cleft." Seven different Salmonella typhimurium phages were used to study if there exist homologous regions in the
active site of these phages and to compare these active sites with that of the P22 tailspike protein.
Role: PI
Pending
S06 GM 50695-04 Villafane (PI) 06/01/03-05/31/05
NIH/GMS/MBRS
Defining the LPS Interaction with Proteins, 2.
These studies are aimed at defining which amino acids are involved in the binding and catalysis of the P22
tailspike protein which is an LPS-binding protein.
Role: PI
NIH/GMS/MBRS
Defining the LPS Interaction with Proteins, 1.
These studies are aimed at defining which amino acids are involved in the binding and catalysis of the P22 tailspike protein which is an LPS-binding protein.
Role: PI
BRIN PR Research award 2002 1/1/02-12/31/02
Modular Nature of Phage Tailspike Proteins
Principal Investigator/Program Director (Last, first, middle): Manual Martinez-Maldonado,MD
Use was made of one bacterial virus that previous studies by the Pi hadT indicated that there were functional homologies between that of the P22 standard virus and the new phage epsilon-34. Studies were aimed at determining what aspects of this new virus tail were similar to those of the P22 tail.
Role: PI
USDA Moore (PI) 6/1/95-5/31/96
Molecular Study of Pasteurella Toxin Production
Molecular analysis of the epitope responsible for the toxic effect of the Pasteurella bacteria.
Role: Co-Investigator
