A Rao

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A Rao

A Rao

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Biography

University of California Riverside - Science

Professor at University of California-Riverside
A.L.N.
Rao
Riverside, California
Experienced Professor with a demonstrated history of working in the higher education industry. Skilled in Molecular Virology, host-viral pathogen interactions, Bioinformatics, Life Sciences, Microscopy, Genetics, and Cell Biology. Strong education professional with a Doctor of Philosophy (Ph.D.) focused in Plant Pathology from Waite Institute, University of Adelaide.

Experience

  • University of California

    PROFESSOR

    A worked at University of California as a PROFESSOR

Education

  • Indian Agricultural Research Institute, New Delhi

    Master of Science (M.Sc.)

    Plant Pathology

  • Waite Institute, University of Adelaide

    Doctor of Philosophy (Ph.D.)

    Plant Pathology

Publications

  • Integration of replication and assembly of infectious virions in plant RNA viruses

    Current Opinion in Virology

  • Integration of replication and assembly of infectious virions in plant RNA viruses

    Current Opinion in Virology

  • Functional analysis of the N-terminal basic motif of a eukaryotic satellite RNA virus capsid protein in replication and packaging

    Scientific Reports

    Efficient replication and assembly of virus particles are integral to the establishment of infection. In addition to the primary role of the capsid protein (CP) in encapsidating the RNA progeny, experimental evidence on positive sense single-stranded RNA viruses suggests that the CP also regulates RNA synthesis. Here, we demonstrate that replication of Satellite tobacco mosaic virus (STMV) is controlled by the cooperative interaction between STMV CP and the helper virus (HV) Tobacco mosaic virus (TMV) replicase. We identified that the STMV CP-HV replicase interaction requires a positively charged residue at the third position (3R) in the N-terminal 13 amino acid (aa) motif. Far-Northwestern blotting showed that STMV CP promotes binding between HV-replicase and STMV RNA. An STMV CP variant having an arginine to alanine substitution at position 3 in the N-terminal 13aa motif abolished replicase-CP binding. The N-terminal 13aa motif of the CP bearing alanine substitutions for positively charged residues located at positions 5, 7, 10 and 11 are defective in packaging full-length STMV, but can package a truncated STMV RNA lacking the 3′ terminal 150 nt region. These findings provide insights into the mechanism underlying the regulation of STMV replication and packaging.

  • Integration of replication and assembly of infectious virions in plant RNA viruses

    Current Opinion in Virology

  • Functional analysis of the N-terminal basic motif of a eukaryotic satellite RNA virus capsid protein in replication and packaging

    Scientific Reports

    Efficient replication and assembly of virus particles are integral to the establishment of infection. In addition to the primary role of the capsid protein (CP) in encapsidating the RNA progeny, experimental evidence on positive sense single-stranded RNA viruses suggests that the CP also regulates RNA synthesis. Here, we demonstrate that replication of Satellite tobacco mosaic virus (STMV) is controlled by the cooperative interaction between STMV CP and the helper virus (HV) Tobacco mosaic virus (TMV) replicase. We identified that the STMV CP-HV replicase interaction requires a positively charged residue at the third position (3R) in the N-terminal 13 amino acid (aa) motif. Far-Northwestern blotting showed that STMV CP promotes binding between HV-replicase and STMV RNA. An STMV CP variant having an arginine to alanine substitution at position 3 in the N-terminal 13aa motif abolished replicase-CP binding. The N-terminal 13aa motif of the CP bearing alanine substitutions for positively charged residues located at positions 5, 7, 10 and 11 are defective in packaging full-length STMV, but can package a truncated STMV RNA lacking the 3′ terminal 150 nt region. These findings provide insights into the mechanism underlying the regulation of STMV replication and packaging.

  • Functionalityofhostproteinsin Cucumber mosaicvirus replication: GAPDHisobligatorytopromoteinteractionbetween replication-associatedproteins

    Virology

    Here, we evaluated the role of two host proteins, a Bromo domain containing RNA binding protein(BRP1)and Glyceraldehyde3-phosphatedehydrogenase(GAPDH),in the replication of Cucumber mosaic virus (CMV). LC-MS/MS analysis of host/viral proteins pulldown against BRP1 from CMV-infected plants co-infiltrated with BRP1-FLAG agroconstruct identified that BRP1specifically interacts with a ten amino acid motif (843-SPQDVVPLVR-852) encompassing the helicase domain of replicase proteinp1a.The interaction between BRP1and p1a was subsequently confirmed using a BiFC assay. Among fourteen other host proteins identified to interact with BRP1 during CMV infection, six were found to block accumulation of viral progeny in Arabidopsisthaliana lines defective in each of these host proteins.Additional BiFC assays followed by trans-complementation assays identified that plant lines defective in the expression of GAPDH blocked CMV replication by interfering with p1a:p2a interaction. Distinct roles of BRP1and GAPDH in the replication of CMV are discussed.

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BIO 123

4(5)

  • Level:
  • Credit hours: 0

BIOL 123

3.7(3)

  • Level:
  • Credit hours: 0

PPLA 123

5(1)

  • Level:
  • Credit hours: 0

VIRO

1(1)

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  • Credit hours: 0

VIROLOGY

3.5(1)

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VIROLOGY 12

1.5(1)

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BIOLA 107

5(1)

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