2025

• Zhu, J., Sha, J., Batra, H., Jain, S., Wu, X., Hendrix, E.K., Kilgore, P.B., Sun, K., Plante, K.S., Plante, J.A., Walker, J., Tao, P., Chopra, A.K. and Rao, V.B. (2025), A Modular
  Bacteriophage T4 Nanoparticle Platform Enables Rapid Design of Dual COVID-19-Flu Mucosal Vaccines. Small Sci., 5: 2400580. (Frontispiece Page).

2024

• Zhu, J., Tao, P., Chopra, A. K., and Rao, V. B. (2024). Bacteriophage T4 as a Protein-Based, Adjuvant- and Needle-Free, Mucosal Pandemic Vaccine Design Platform. Ann. Rev. Virol. 11(1):395-420.

• Wang, S., Kuang, S., Song, H. et al., Rao, V. B., and Tao, P. (2024). The role of TIR domain-containing proteins in bacterial defense against phages. Nature Communications, 15, 7384. 

• Jain, S., Uritskiy, G., Mahalingam, M., Batra, H., Chand, S., Trinh, H. V., Beck, C., Shin, W.-H., Alsalmi, W., Kijak, G., Eller, L. A., Kim, J., Kihara, D., Tovanabutra, S., Ferrari, G., Robb, M. L., Rao, M., and Rao, V. B. (2024). A remarkable genetic shift in a transmitted/founder virus broadens antibody responses against HIV-1. eLife, 13.

2023

• Prévost, J., Chen, Y., Zhou, F. et al. (2023). Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir. Nature Communications, 14, 6710. 

• Fokine, A., Islam, M.Z., Fang, Q., Chen, Z., Sun, L. and Rao, V.B. (2023). Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages. Viruses, 15, 1517. (Cover Page)

• Zhu, J., Batra, H., Ananthaswamy, N., Mahalingam, M., Tao, P., Wu, X., Guo, W., Fokine, A. and Rao, V.B. (2023). Design of Bacteriophage T4-based Artificial Viral Vectors for Human Genome Remodeling. Nature Communications 14:2928. 

• Rao, V. B., Fokine, A, Fang, Q, Shao, Q. (2023). Bacteriophage T4 Head: Structure, Assembly, and Genome Packaging. Viruses, 14;15(2). 

2022

• Fang, Q., Tang, Wei-Chun, Fokine, A., Mahalingam, M., Shao, Q., Rossmann, M. G., and Rao, V. B. (2022). Structures of a large prolate virus capsid in unexpanded and expanded states generate insights into the icosahedral virus assembly. PNAS, 119 (40): e2203272119.

• Rao, V. B., and Zhu J. (2022). Bacteriophage T4 as a nanovehicle for delivery of genes and therapeutics into human cells. Curr. Opin. Virol. 55:101255. (Cover Page)

• Zhu, J., Jain, S., Sha, J., Batra, H., Ananthaswamy, N., Kilgore, P. B., Hendrix, E. K., Hosakote, Y. M., Wu, X., Olano, J. P., Kayode, A., Galindo, C. L., Banga, S., Drelich, A., Tat, V., Tseng, C.-Te., K., Chopra A. K., Rao, V. B. (2022). A bacteriophage-Based, highly efficacious, needle- and adjuvant-free, mucosal COVID-19 vaccine. mBio, 13.

2021

• Li Dai, Digvijay Singh, Suoang Lu, Vishal Kottadiel, Reza Vafabakhsh, Marthandan Mahalingam, Yann R. Chemla, Taekjip Ha, Venigalla B. Rao (2021). A viral genome packaging ring-ATPase is a flexibly coordinated pentamer. Nature Communications, 12:6548.

• Zhu, Neeti Ananthaswamy, Swati Jain, Himanshu Batra, Wei-Chun Tang, Douglass A. Lewry, Michael L. Richards, Sunil A. David, Paul B. Kilgore, Jian Sha, Aleksandra Drelich, Chien-Te K. Tseng, Ashok K. Chopra, Venigalla B. Rao (2021). A Universal Bacteriophage T4 Nanoparticle Platform to Design Multiplex SARS-CoV-2 Vaccine Candidates by CRISPR Engineering. Science Advances, 7(37): eabh1547.

• Rao, V. B., Fokine, A. and Fang, Q. (2021). The Remarkable Viral Portal Vertex: a plausible model for mechanism. Curr. Opin. Virol. 52:65-73.

• Son BK, Patterson-West J, Arroyo-Mendoza J, Ramachandran R, Iben JR, Zhu J, Venigalla B. Rao, Dimitriadis EK, Hinton DM, (2021). A phage-encoded Nucleoid Associated Protein condenses both host and phage DNA and depresses H-NS silencing. Nucleic Acids Research, 49(16):9229-9245.

• Xiaorong Wu, Jingen Zhu, Pan Tao, Venigalla B. Rao (2021). Bacteriophage T4 Escapes CRISPR Attack by Mini-homology Recombination and Repair. mBio, 12. 

2020

• Liu Y, Dai L, Dong J, Chen C, Zhu J, Rao VB, Tao P. (2020). Covalent Modifications of the Bacteriophage Genome Confer a Degree of Resistance to Bacterial CRISPR Systems. J. Virology, 9;94(23).

• Mo Y, Keller N, delToro D, Ananthaswamy N, Harvey SC, Rao VB, Smith DE. (2020). Function of a viral genome packaging motor from bacteriophage T4 is insensitive to DNA sequence. Nucleic Acids Res. 48(20):11602-11614. 

• Fang, Q., Tang, W. C., Tao, P., Mahalingam, M., Fokine, A., Rossmann, M. G., Rao, V. B. (2020). Structural morphing in a symmetry-mismatched viral vertex. Nature Communications, 6;11(1):1713.

2019

• Islam, M. Z., Fokine, A., Mahalingam, M., Zhang, Z., Garcia-Doval, C., van Raaij, M. J., Rossmann, M. G., Rao, V. B. (2019). Molecular anatomy of the receptor binding module of a bacteriophage long tail fiber. PLoS Pathogens, Dec 19;15(12).

• Zhu, J., Tao, P., Mahalingam, M., Sha, J., Kilgore, P., Chopra, A. K. and Rao, V. (2019). A prokaryotic eukaryotic hybrid viral vector for delivery of large cargos of genes and proteins into human cells. Science Advances, 5(8):eaax0064.

• Ananthaswamy, N., Fang, Q., AlSalmi,W., Jain, S., Chen, Z., Klose, T., Sun, Y., Liu, Y., Mahalingam, M., Chand, S., Tovanabutra, S., Robb, M., Rossmann, M.and Rao, V. B. (2019). A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer. Nature Communications, 10(1):873.

2018

• Ordyan, M., Alam, I., Mahalingam, M., Rao, V. B. and Smith, D. E. (2018). Nucleotide-dependent DNA gripping and an end-clamp mechanism regulate the bacteriophage T4 viral packaging motor. Nature Communications, 9(1):5434.

• Tao, P., Mahalingam, M., Zhu, J., Moayeri, M., Sha, J., Lawrence, W. S., Leppla, S. H., Chopra, A. K. and Rao, V. B. (2018). A bacteriophage T4 nanoparticle based dual vaccine against anthrax and plague. mBio, 9(5):e01926-18.
  This paper was highlighted in NIH Research Matters, October 30, 2018 and Newsweek, October 26, 2018.

• Tao, P., Zhu, J., Mahalingam, M., Batra, H. and Rao, V. B. (2018). Bacteriophage T4 nanoparticles for vaccine delivery against infectious diseases. Adv. Drug Delivery Rev. 18: 30164-79.

• Tao, P., Wu, X. and Rao, V.B. (2018). Unexpected evolutionary benefit to phages imparted by bacterial CRISPR-Cas9. Science Advances, 4(2):eaar4134.
  This paper was highlighted in the February 16, 2018 issue of Science.

2017

• Lin, S., Alam, T.I., Kottadiel, V., VanGessel, C.J., Tang, W-C., Chemla, Y.R., and Rao, V.B. (2017). Altering the speed of a DNA packaging motor from bacteriophage T4. Nucleic Acids Research. 45(19):11437-11448.

• Chen, Z., Sun, L., Zhang, Z., Fokine, A., Padilla-Sanchez, V., Hanein, D., Jiang, W., Rossmann, M.G., and Rao, V.B. (2017). Cryo-EM structure of the bacteriophage T4 isometric head at 3.3-Å resolution and its relevance to the assembly of icosahedral viruses. PNAS, 114(39):E8184-E8193.

• Tao, P., Wu, X., Tang, W.C., Zhu, J., and Rao, V.B. (2017). Engineering of Bacteriophage T4 Genome Using CRISPR-Cas9. ACS Synth Biol. 6(10):1952-1961.

• Chand, S., Messina, E.L., AlSalmi, W., Ananthaswamy, N., Gao, G., Uritskiy, G., Padilla-Sanchez, V., Mahalingam, M., Peachman, K.K., Robb, M.L., Rao, M., and Rao, V.B. (2017). Glycosylation and oligomeric state of envelope protein might influence HIV-1 virion capture by α4β7 integrin. Virology, 508:199-212.

• Kim, J., Jobe, O., Peachman, K.K., Michael, N.L., Robb, M.L., Rao, M., and Rao, V.B. (2017). Quantitative analyses reveal distinct sensitivities of the capture of HIV-1 primary viruses and pseudoviruses to broadly neutralizing antibodies. Virology 508:188-198. (This paper was highlighted in the Virology Highlights Blog, here.) 

• Tao, P., Mahalingam, M., Zhu, J., Moayeri, M., Kirtley, M., Fitts, E., Andersson, J., Lawrence, W., Leppla, S., Chopra, A., and Rao, V.B. (2017). A Bivalent Anthrax-Plague Vaccine That Can Protect Against Two Tier-1 Bioterror Pathogens, Bacillus anthracis and Yersinia pestis. Front. Immunol. 8: 687.

2016

• Gao, S., Zhang, L., and Rao, V.B. (2016). Exclusion of small terminase mediated DNA threading models for genome packaging in bacteriophage T4. Nucleic Acids Res. 44(9):4425-39.

2015

• Rao, V.B., and Feiss, M. (2015). Mechanisms of DNA Packaging in Large Double Stranded DNA Viruses. Ann. Rev. Virology, 2(1):351-378.

• AlSalmi, W., Mahalingam, M., Ananthaswamy, N., Hamlin, C., Flores, D., Gao, G., and Rao, V.B. (2015). New Approach to Produce HIV-1 Envelope Trimers: both cleavage and proper glycosylation are essential to generate authentic trimers. J. Biol. Chem. 290:19780-95.

• Sun, L., Zhang, X., Gao, S., Rao, P.A., Padilla-Sanchez, V., Chen, Z., Sun, S., Xiang, Y., Subramaniam, S., Rao, V.B., and Rossmann, M.G. (2015). Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution. Nature Communications, 6:7548.

2014

• Vafabakhsh R, Kondabagil K, Earnest T, Lee KS, Zhang Z, Dai L, Dahmen KA, Rao VB, Ha T. (2014). Single-molecule packaging initiation in real time by a viral DNA packaging machine from bacteriophage T4. PNAS, 111:15096-101.

• Miglioria, A.D., Keller, N., Alam, T.I., Mahalingam, M., Rao, V.B., Arya, G., and Smith, D.E. (2014). Evidence for an electrostatic mechanism of force generation by the bacteriophage T4 DNA packaging motor. Nature Communications, 5:4173, 1-9.

2013

• Padilla-Sanchez, V., Gao, S., Kim, H.R., Kihara, D., Sun, L., Rossmann, M.G., and Rao, V.B. (2013). Structure-function analysis of the DNA translocating portal of the bacteriophage T4 packaging machine. J. Mol. Biol. 426:1019-1038.

• Tao, P., Mahalingam, M., Kirtley, M., van Lier, C.J., Sha, J., Yeager, L.A., Chopra, A.K., and Rao, V.B. (2013). Mutated and bacteriophage T4 nanoparticle arrayed F1-V immunogens from Yersinia pestis as next generation plague vaccines. PLOS Pathogens, 9(7):e1003495.

• Tao, P., Mahalingam, M., Marasa, B., Chopra, A., and Rao, V.B. (2013). In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine. PNAS, 110:5846-5851.

2012

• Kottadiel, V.I., Rao, V.B., and Chemla, Y.R. (2012). The dynamic pause-unpackaging state, an off-translocation recovery state of a DNA packaging motor from bacteriophage T4. PNAS, 109:20000-20005.

• Black, L.W., and Rao, V.B. (2012). Structure, Assembly, and DNA packaging of bacteriophage T4 head. Adv. Virus Res. 82:119-153. (Cover Page)

• Sun, S., Gao, S., Kondabagil, K., Xiang, Y., Rossmann, M.G., and Rao, V.B. (2012). Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages. PNAS, 109(3):817-22.

2011

• Ghosh-Kumar, M., Alam, T.I., Draper, B., Stack, J., and Rao, V.B. (2011). Regulation by Interdomain Communication of a Headful Packaging Nuclease from Bacteriophage T4. Nucleic Acids Res. 39:2742-2755.

• Zhang, Z., Kottadiel, V., Vafabakhsh, R., Li, Dai, Chemla, Y.R., Ha, T.J., and Rao, V.B. (2011). A promiscuous DNA packaging machine from bacteriophage T4. PLOS Biology, 9(2):e10005929.
  (This article was a “Research Highlight” in Nature Reviews Microbiology, 2011 Vol.9, Issue 4, here.)

2010

• Sun, S., Rao, V.B., and Rossmann, M. (2010). Genome packaging in viruses. Curr.Opin. Struct. Biol. 20 (1):114-120.

• Li, Q., Fokine, A., O’Donnell, E., Rao, V.B., and Rossmann, M.R. (2010). The Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages. J. Mol. Biol. 395:728-41.

2009

• Rao, V.B. (2009). A virus DNA gate: zipping and unzipping the packed viral genome. PNAS, 106: 8403-8404.

2008

• Sun, S., Kondabagil, K., Draper, B., Alam, I.T., Baumann, V., Zhang, Z., Hegde, S., Fokine, A., Rossmann, M.G., and Rao, V.B. (2008). The atomic structure of bacteriophage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces. Cell 135:1251-1262. (This paper was featured as a Leading Edge “Preview” in the same issue, here.) 

• Rao, V.B., and Feiss, M. (2008). The bacteriophage DNA packaging motor. Ann. Rev. Genetics, 42:642-681.

2007

• Fuller, D.N., Raymer, D.M., Kottadiel, V.I., Rao, V.B., and Smith, D.E. (2007). Single Phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability. PNAS, 104:16868-16873.

• Sun, S., Kondabagil, K., Gentz, P.M., Rossmann, M.G., and Rao, V.B. (2007). The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids. Mol. Cell. 25(6):943-949.

• Li, Q., Shivachandra, S.B., Zhang, Z., and Rao, V.B. (2007). Assembly of the Small Outer Capsid protein, Soc, on bacteriophage T4: a novel system for high density display of multiple large anthrax toxins and foreign proteins on phage capsid. J. Mol. Biol. 370:1006-1019. (Cover Page)

• Draper, B., and Rao, V.B. (2007). An ATP hydrolysis sensor in the DNA packaging motor from bacteriophage T4 suggests inchworm type translocation mechanism. J. Mol. Biol. 367:79-94.

2006

• Kondabagil, K.R., Zhang, Z.B., and Rao, V.B. (2006). The DNA translocating ATPase of bacteriophage T4 packaging motor. J. Mol. Biol. 363:786-799.

• Kondabagil, K.R., and Rao, V.B. (2006). A critical coiled coil motif in the small terminase, gp16, from bacteriophage T4: insights into DNA packaging initiation and assembly of packaging motor. J. Mol. Biol. 358:67-82.

• Shivachandra, S.B., Rao, M., Janosi, L., Sathaliyawala, T., Matyas, G.R., Alving, C.R., Leppla, S.H., and Rao, V.B. (2006). In vitro binding of anthrax protective antigen on bacteriophage T4 capsid surface through Hoc-capsid interactions: a strategy for efficient display of large full-length proteins. Virology, 345:190-198.

• Mitchell, M., and Rao, V.B. (2006). Functional analysis of the bacteriophage T4 DNA packaging ATPase motor. J. Biol. Chem. 281:518-527.

2005 and Earlier

• Fokine, A., Chipman, P., Leiman, P., Mesyanzhimov, V., Rao, V., and Rossmann, M. (2004). Molecular architecture of the prolate head of bacteriophage T4. PNAS, 101:6003-6008.

• Rentas, F., and Rao, V.B. (2003). Defining the Bacteriophage T4 DNA Packaging Machine: evidence for a C-terminal DNA cleavage domain in the large terminase/packaging protein gp17. J. Mol. Biol. 334:37-52.

• Goetzinger, K., and Rao, V.B. (2003). Defining the ATPase center of bacteriophage T4 DNA packaging machine: requirement for a catalytic glutamate in the large terminase protein gp17. J. Mol. Biol. 331:139-154.

• Mitchell, M., Matsuzaki, S., Imai, S., and Rao, V.B. (2002). Sequence analysis of bacteriophage T4 DNA-packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Res. 30:4009-4021.

• Rao, V.B., and Mitchell, M. (2001). The N-terminal ATPase site in the large Terminase Protein Gp17 is critically required for DNA packaging in bacteriophage T4. J. Mol. Biol. 314:411-421.

• Leffers, G., and Rao, V.B. (2000). Biochemical Characterization of an ATPase Activity Associated with the Large Packaging Subunit Gp17 from Bacteriophage T4. J. Biol. Chem. 275:37127-37136.

• Kuebler, D., and Rao, V.B. (1998). Functional Analysis of the DNA Packaging/Terminase Protein Gp17 from Bacteriophage T4. J. Mol. Biol. 281:803-814.

• Jiang, J., Abu-Shilbayeh, L., and Rao, V.B. (1997). Display of a PorA Peptide from Neisseria meningitidis on the Bacteriophage T4 Capsid Surface. Infection and Immunity, 65:4770-4777.

• Leffers, G., and Rao, V.B. (1996). A discontinuous headful packaging model for packaging less than headful length DNA molecules by bacteriophage T4. J. Mol. Biol. 258:839-850.

• Rao, V.B., Thaker, V., and Black, L.W. (1992). A phage T4 in vitro packaging system for cloning long DNA molecules. Gene 113:25-33.

• Rao, V.B., and Black, L.W. (1988). Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4; Construction of a defined in vitro DNA packaging system using purified terminase proteins. J. Mol. Biol. 200:475-485.

• Rao, V.B., and Black, L.W. (1985). Evidence that a phage T4 DNA packaging enzyme is a processed form of the major capsid gene product. Cell 42:967-977.

• Rao, V.B., and Black, L.W. (1985). DNA packaging of bacteriophage T4 proheads in vitro: Evidence that prohead expansion is not coupled to DNA packaging.J. Mol. Biol. 185:565-578.