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Structural and Computational Biology and Molecular Biophysics

Houston, Texas

A BCM research lab.
Structural and Computational Biology & Molecular Biophysics
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B.V.V. Prasad, Ph.D.

B. V. Venkataram Prasad, Ph.D.Professor, Biochemistry and Molecular Biology

SCBMB Executive Committee Member

Baylor College of Medicine


Ph.D. Biochemistry, University of Arizona

Research Interests:

Research in Dr. Prasad's laboratory is focused on determining structure-function relationships in medically important viruses that are pathogens to humans and other animals. The current focus is on viruses that are causative agents of endemic severe diarrhea in humans. These viruses include rotavirus, calicivirus, and Norwalk virus. Rotavirus is the major pathogen of infantile gastroentritis. More than a million children die every year worldwide because of rotaviral gastroentritis. Recently, several other viruses, including calicivirus and Norwalk virus, also have been shown to be causative agents of pediatric diarrhea. Our three-dimensional structural analyses have provided architectural descriptions of these viruses. Our studies using monoclonal antibodies, reassortants, and baculovirus-expressed virus-like particles have provided insights into the molecular mechanisms of cell entry, infectivity, transcription, and assembly of rotavirus. Rotavirus is a member of the virus family Reoviridae. Comparative structural analysis of other members in this family, such as blue-tongue virus and aquareovirus, is being carried out to provide a unified picture of the molecular mechanisms underlying the morphogenesis and pathogenesis of these large, complex, multi-layered viruses.

We perform our three-dimensional structural analyses by using electron cryomicroscopy and computer image-processing techniques. In favorable circumstances, x-ray crystallography is being used to study either entire virus particles or their protein components. We have recently determined the structure of Norwalk virus capsids to atomic resolution by using x-ray crystallographic techniques.

Low dose electron micrograph of a double-shelled rotavirus embedded in vitreous ice.

Low-dose electron micrograph of double-shelled rotavirus particles embedded in vitreous ice.
Arrows indicate the spikes emanating from the surface of the virions.

Prasad Illustration 2

Surface representation of the three-dimensional structure of the double-shelled rotavirus.

Selected Publications:

  • Zheng B, Yao Y, Liu Z, Deng L, Anglin JL, Jiang H, Prasad BV and Song Y. Crystallographic Investigation and Selective Inhibition of Mutant Isocitrate Deyhdrogenase. ACS Med Chem Lett, 4(6):542-546 (2013). PubMed
  • Muhaxihiri Z, Deng L, Shanker S, Sankaran B, Estes MK, Palzkill T, Song Y and Prasad BV. Structural basis of substrate specificity and protease inhibition in Norwalk virus. J Virol, 87(8):4281-92 (2013). PubMed
  • Hu L, Crawford SE, Czako R, Cortes-Penfield NW, Smith DF Le Pendu J, Estes MK and Prasad BV. Cell attachment to protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen. Nature, 485(7397)256-9 (2012). PubMed
  • Prasad BV and Schmid MF. Principles of virus structural organization. Adv Exp Med Biol, 726:17-47 (2012). PubMed
  • Yao Y, Chen P, Diao J, Cheng G, Deng L, Anglin JL, Prasad BV and Song Y. Selective inhibitors of histone methyltransferase DOT1L: design, synthesis, and crystallographic studies. J Am Chem Soc, 133(42):16746-9 (2011). PubMed
  • Shanker, S., Choi, J.M., Sankaran, B., Atmar, R.L., Estes, M.K. and Prasad, B.V. Structural analysis of histo-blood group antigen binding specificity in a norovirus GII, 4 epidemic variant: implications for epochal evolution. J Virol, 85(17):8635-45 (2011). PubMed
  • Baker M and Prasad BV. Rotavirus cell entry. Curr Top Microbiol Immunol, 343:121-48 (2010). PubMed

For more publications, see listing on PubMed.

Contact Information:

Department: Biochemistry and Molecular Biology
Address: Baylor College of Medicine
One Baylor Plaza
Room N410
Houston, Texas 77030
Phone: 713-798-5686
Fax: 713-798-1625
Additional Links: Department of Biochemistry

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