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| Name |
Summers, Michael F. |
| Location
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University of Maryland, Baltimore County |
| Primary Field
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Biophysics and Computational Biology |
| Secondary Field
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Biochemistry |
 Election Citation
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Summers is a leader in the structural and mechanistic aspects of retroviral genome packaging, maturation, and virus assembly. His findings have provided a long-sought explanation for how retroviruses selectively package a diploid genome and how Gag protein is targeted to the plasma membrane for virus assembly.
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Research Interests
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Michael Summers' laboratory uses NMR methods to study the structural determinants and mechanisms of retroviral genome packaging and virus assembly. They have determined the 3D structures of all of the major structural proteins of HIV-1, and have identified novel mechanisms for inhibiting the virus by zinc-ejecting and capsid-binding small molecules. Current studies focus on understanding how the matrix domain of the HIV-1 Gag polyprotein protein and it's interactions with cellular constituents regulates the targeting of Gag to assembly sites on the plasma membrane. A major emphasis also focuses on developing NMR approaches to study relatively large RNAs (up to ~700 nucleotides), enabling structural studies of the 5¿-leader of the HIV-1 genome. The 350-nucleotide HIV-1 leader, the most conserved region of the viral genome, regulates early- and late-phase RNA-dependent replication activities by what appears to be a structure-dependent mechanism. Recent NMR studies have led to understanding of how unspliced dimeric genomes, but not the highly abundant spliced viral mRNAs, are specifically and efficiently selected for packaging during virus assembly. Ongoing studies of Gag:5¿-leader RNA interactions are aimed at providing structural insights into the ribonucleoprotein complex that is trafficked to the plasma membrane and nucleates virus assembly.
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