Gender	Male
E-mail	john.blaho@mssm.edu
	blaholab@mssm.edu
Education and Training	Ph.D., University of Alabama Schools of Medicine and Dentistry
	B.E., Manhattan College
	Cert, University of Vienna
Awards	1996 Young Investigator National Foundation for Infectious Diseases
	1996 Junior Faculty Research Award American Cancer Society
	1994 Markey Research Fellow The Lucille P. Markey Charitable Trust
	1991 Visiting Lecturer in the Department of Virology University of Turku, Turku, Finland
	1989 - 1991 U.S.P.H.S. Postdoctoral Trainee, Committee on Virology University of Chicago
	1988 First Place Award at Graduate Student Research Day Birmingham Chapter of Sigma Xi, The Research Society
	1987 Bertram Marx Graduate Student Award for Research in Cancer-related Areas Comprehensive Cancer Center, University of Alabama at Birmingham
	1987 Phi Lambda Upsilon National Chemistry Honor Society
	1986 Visiting Scientist in the Department of Microbiology Cornell University Medical College, New York, NY
	1983 Graduate Student Fellowship University of Alabama at Birmingham
	1982 Tau Beta Pi National Engineering Honor Society
	1982 Undergraduate Research Fellowship in Chemical Engineering Clarkson College of Technology, Potsdam, NY
	1982 Epsilon Sigma Pi Honor Society Manhattan College

John Blaho, Ph.D., has focused his research on the herpes simplex virus (HSV), with the goal of understanding the molecular events involved in the regulation of the replication of this human virus and also the mechanisms by which the virus causes cell death. Herpes simplex viruses are neurotropic viruses that cause a variety of infections, remain latent in the neurons of their host for life, and can be reactivated at any time to cause lesions at or near the initial site of infection. In 1999, Aubert and Blaho discovered that the major regulatory protein of HSV is required for the prevention of programmed cell death (apoptosis) in infected human cells.

Blaho and his associates have also defined the biology of the major protein component of the HSV virion and have discovered that HSV first induces and then prevents apoptosis during its replication cycle, a process group has termed "Apoptosis Modulation by HSV." An understanding of the processes of replication and reactivation is of great clinical import because of the possibility of designing effective therapy that would interfere with one or another molecular pathway as a way to cure HSV infection. Blaho and his colleagues also hope to translate their findings into novel strategies for limiting uncontrolled cell growth such as is found in tumor cells by using a process they recently discovered called "viral oncoapoptosis."

Since coming to Mount Sinai, Blaho has played a significant role in the teaching activities of the Department of Microbiology. He has served on numerous student advisory and examination committees and has been responsible for the training of more than twenty Ph.D. and M.D./Ph.D. students. He has directed the Graduate Microbiology Training Program and since 1998 has been both the director of the "Introduction to Microbiology" core Graduate School course and codirector of the Graduate School's Microbiology Multidisciplinary Training Area. In 1999, Blaho led the preparation of the training grant proposal, funded by the NIH, that established a program in Mechanisms of Virus-Host Interactions. An active participant in science at the national level, Blaho serves on the editorial boards of the major virology journals and is also a permanent member of the NIH virology study section.

Except from: Niss, B. J. and Aufses, A. H. Teaching Tomorrow's Medicine Today: The Mount Sinai School of Medicine, 1963-2003. New University Press, New York, NY.

Education and Training	Ph.D., University of Alabama Schools of Medicine and Dentistry
	B.E., Manhattan College
	Cert, University of Vienna

Molecular Virology / Regulation of Herpes Simplex Virus Replication/ Apoptosis and Signal Transduction
Herpes simplex viruses cause a variety of infections, remain latent in their host for life, and can be reactivated to cause lesions at or near the site of infection. While the mechanism of viral reactivation from the latent state remains unclear, it is likely that the process involves the transfer of a neuronal signal to the viral replication machinery. The goal of our laboratory is to understand the molecular mechanisms involved in the regulation of the replication of human herpes simplex virus. We use biochemical and molecular genetic techniques to identify and characterize the viral and cellular gene products which are important in the regulatory processes. We are currently focusing on viral proteins which regulate the expression of HSV genes at either the transcriptional or posttranscriptional level. We are also examining viral proteins which structurally participate in the formation of the virion. These proteins were recently shown to possess novel posttranslational modifications and at least one cellular enzyme has been identified which participates in the modification reaction. The role that these moieties play in HSV replication is a major focus of our research. In the long term, we hope to define, at the molecular level, the life-cycle of this important human pathogen.

Future research opportunities:

(i) Viral Molecular Genetics. Our laboratory has the capacity to generate recombinant herpes simplex viruses using state-of-the-art molecular biology tools. An assessment of the replication capacity of specifically mutated viruses enables us to define the exact regulatory functions of specific HSV gene products.

(ii) Signal Transduction and Apoptosis. One long-term goal of our laboratory is to define the cellular signaling mechanisms which regulate the synthesis and modification of HSV proteins during infection. We shall identify and determine the function of the factors responsible for these prospective signaling processes. In addition, we intend to determine all HSV components involved in the modulation of apoptosis in infected cells.

(iii) Structural Biology of Viral Proteins. The posttranslationally modified structures (tyrosine phosphorylation, nucleotidylation, and [ADP-ribosyl]ation) of HSV proteins are studied in our laboratory using protein chemistry analyses. The molecular basis of the transferred adducts shall be determined using physical-biochemistry techniques, including spectroscopic methods.

Aubert M, Blaho JA. Viral oncoapoptosis of human tumor cells. Gene Therapy 2003; 10: 1437-45.

Goodkin M, Ting A, Blaho JA. NF-<font face='Symbol'>k</font>B is required for apoptosis prevention during HSV-1 infection. J Virol 2003; 77: 7261-80.

Sanfilippo CM, Chirimuuta FN, Blaho JA. Herpes simplex virus type 1 immediate-early gene expression is required for the induction of apoptosis in human epithelial HEp-2 cells. J Virol 2004 Jan; 78(1): 224-39.

Sanfilippo CM, Lombardozzi RC, Chirimuuta FN, Blaho JA. Herpes simplex virus 1 infection is required to produce ICP27 immunoreactive triplet forms when ribosomal aminoacyl-tRNA translocation is blocked by cycloheximide. Virology 2004 Jul 1; 324(2): 554-66.

Yedowitz JC, Blaho JA. Herpes simplex virus 2 modulates apoptosis and stimulates NF-kappaB nuclear translocation during infection in human epithelial HEp-2 cells. Virology 2005 Nov 25; 342(2): 297-310.

Nguyen ML, Kraft RM, Blaho JA. African green monkey kidney Vero cells require de novo protein synthesis for efficient herpes simplex virus 1-dependent apoptosis. Virology 2005 Jun 5; 336(2): 274-90.

Yedowitz JC, Kotsakis A, Schlegel EF, Blaho JA. Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import. J Virol 2005 Apr; 79(8): 4730-43.

Kraft RM, Nguyen ML, Yang XH, Thor AD, Blaho JA. Caspase 3 activation during herpes simplex virus 1 infection. Virus Res 2006 Sep; 120(1-2): 163-75.

Sanfilippo CM, Blaho JA. ICP0 gene expression is a herpes simplex virus type 1 apoptotic trigger. J Virol 2006 Jul; 80(14): 6810-21.

Aubert M, Pomeranz LE, Blaho JA. Herpes simplex virus blocks apoptosis by precluding mitochondrial cytochrome c release independent of caspase activation in infected human epithelial cells. Apoptosis 2007 Jan; 12(1): 19-35.