Virus assembly, structure & evolution
The Hendrix lab studies virus assembly as a means to understand more general questions about protein structure, protein-protein and protein-DNA interactions, mechanisms and regulation of biological assembly, and the role of chaperones in assembly. We use bacteriophages (the dsDNA tailed variety); as our experimental organisms.
Our main effort is on the assembly of the capsids (heads); of phage HK97. This E. coli phage assembles a 420 subunit shell that matures through a remarkable conformational dance that includes proteolytic processing of all the subunits, pumping a DNA chromosome into the empty protein shell, assembling catalytic sites and forming covalent bonds among all the subunits autocatalytically. The result is the ultra-stable "viral chainmail" structure in which covalent protein circles are linked topologically into a continuous "nano-fabric". We study all parts of this assembly pathway, using biochemical and genetic approaches and collaborating with structural biologists.
We also have projects to understand assembly of phage tails and tail fibers, including questions about chaperone-mediated assembly and length determination of homopolymeric structures.
The lab also has a collaborative project on bacteriophage genomics in which we learn about the evolution and population biology of phages. Although not directly related to the interests of the MBSB graduate program, this project brings an evolutionary dimension to our studies of phage structure and assembly mechanisms. It also provides a wealth of different phage types for our collaborative studies with the Conway lab on how different viruses achieve different capsid structures.
PhD 1970, Harvard University
Department of Biological Sciences
University of Pittsburgh
A340A Langley Hall
4249 Fifth Avenue
Pittsburgh, PA 15260
Phone: (412) 624-4674
Fax: (412) 624-4870