HMS Virology

Virology Faculty Member - Max Nibert

Max Nibert

Harvard Medical School
Micro. & Mol. Genetics, Armenise Bldg., Rm. 523
200 Longwood Ave.
Boston, MA 2115
Tel: 617 432 4829
Fax: 617-738-7664

We use dsRNA viruses from the families Reoviridae (primarily orthoreoviruses and rotaviruses), Partitiviridae, and Totiviridae to study fundamental aspects of structure-function relationships in virus particles, virus particle assembly, virus-cell interactions, and viral pathogenesis. Areas of current focus include the following.

Virus entry into cells. We are interested to define the biochemical and biophysical mechanisms by which nonenveloped viruses penetrate the cellular membrane barrier during entry. Since these viruses lack a lipid envelope that they can fuse with the cell’s, mechanisms distinct from fusion are required.

Synthesis, processing, and transport of viral RNA. The genome-enclosing capsid particle of the dsRNA viruses represents a biochemically defined system for RNA-dependent RNA transcription, RNA 5´ capping, and mRNA transport. Though much simpler than the related machinery of cells, this system is providing new insights into the structural and dynamic aspects of these basic processes.

Virus assembly inside cells. The volume of a cell is large compared to the small portion used by most viruses for their assembly. Moreover, the cell is highly compartmentalized with regard to different functions that viruses may need. We are interested to define specific elements of cellular organization that viruses exploit to benefit their own replication. Particular focus is on the content and organization of the cytoplasmic “factories” in which viral replication and assembly occur.

Viral pathogenesis. Orthoreoviruses and rotaviruses are mucosal pathogens that provide powerful models for studies of virus-host interactions and viral pathogenesis. Viral interactions with the mucosal epithelium and the mucosal immune system may be especially useful for the design of more successful mucosal vaccines.

Different approaches are used in our lab as the questions dictate, but biochemical, molecular, and genetic approaches predominate. Collaborations with structural and cellular biologists are embraced to extend our characterizations to higher levels of mechanistic resolution.

Last Update: 10/22/2013


Agosto MA, Ivanovic T, Nibert ML. Mammalian reovirus, a nonfusogenic nonenveloped virus, forms size-selective pores in a model membrane. Proc Natl Acad Sci USA 2006;103:16496-16501.

Ivanovic T, Agosto MA, Chandran K, Nibert ML. A role for molecular chaperone Hsc70 in reovirus outer capsid disassembly. J Biol Chem 2007;282:12210-12219.

Miller CL, Arnold MM, Broering TJ, Eichwald C, Kim J, Dinoso JB, Nibert ML. Virus-derived platforms for visualizing protein associations inside cells. Mol Cell Proteomics 2007;6:1027-1038.

Agosto MA, Middleton JK, Freimont EC, Yin J, Nibert ML. Thermolabilizing pseudoreversions in reovirus outer-capsid protein mu1 rescue the entry defect conferred by a thermostabilizing mutation. J Virol 2007;81:7400-7409.

Ivanovic T, Agosto MA, Zhang L, Chandran K, Harrison SC, Nibert ML. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO J 2008;27:1289-1298.

Ochoa WF, Havens WM, Sinkovits RS, Nibert ML, Ghabrial SA, Baker TS. Partitivirus structure reveals a 120-subunit, helix-rich capsid with distinctive surface arches formed by quasisymmetric coat-protein dimers. Structure 2008;16:776-786.

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