Meeting Abstract

P3.96  Tuesday, Jan. 6  Identification of matrix metalloproteinases in the tobacco hornworm, Manduca sexta GREENLEE, Kendra J.*; VISHNUVARDHAN, Smitha; TOTH, Andy; North Dakota State University; North Dakota State University, F; University of Wisconsin, Superior kendra.greenlee@ndsu.edu

Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases which function to break down various extracellular matrix proteins. The degradation by these proteinases contribute to damage resulting from chronic inflammatory diseases such as arthritis, asthma, and even tumor progression. However, MMPs are also important for proper function of the innate immune system. Larval Manduca sexta, the tobacco hornworm, are a good model organism for studies of innate immunity due to their large body size and hemolymph volume. While two MMPs have been characterized in Drosophila and one has been recently identified in the wax moth, Galleria mellonella, the function of MMPs in insects is relatively unknown. Our hypothesis is that MMPs are important for immune function in M. sexta. To begin testing this hypothesis, we first used degenerative primers to isolate MMP from the fat body of 5th instar caterpillars. We obtained a partial sequence that is 86% similar to MMP-1 in G. mellonella and 93% similar to the putative MMP-1 in the silkworm, Bombyx mori. The homology shared between our gene and MMPs in closely related species, as well as the presence of the highly conserved catalytic zinc-binding region, indicate that the gene we sequenced is an MMP. We predict that this MMP is expressed in immune-related tissues and cells and is upregulated during infection.