Submitted to: Society of Nematologists Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: June 13, 2003
Publication Date: September 1, 2003
Citation: Kovaleva, E.S., Skantar, A.M., Chitwood, D.J. 2004. A matrix metalloproteinase gene from the soybean cyst nematode, heterodera glycines. Journal of Nematology 35(3): 348-349. 2003. Technical Abstract: Despite considerable attention given to proteases as good targets for nematode control strategies, genes encoding metalloproteinases (MP) from plant-parasitic nematodes have not yet been characterized. The available information about MP sequences is restricted by several fragments beyond the catalytic domain of the enzyme. Because the majority of hatching enzymes from non-nematode species are MPs, this class is particularly attractive for study in plant-parasitic nematodes. Here we report the isolation and characterization of a full-length mRNA clone from the soybean cyst nematode Heterodera glycines encoding a putative matrix metalloproteinase (Hg-MMP). The deduced preproenzyme with molecular mass of 65.9 kilodalton shares the major structural characteristics of interstitial collagenase M10A subfamily. The catalytic domain includes the three histidine residues involved in coordination of the catalytic zinc atom, a catalytic glutamic acid residue, and a methionine turn common for MPs. The catalytic domain of Hg-MMP exhibits limited homology to corresponding proteases from plants, including host plant Glycine max , and to several hatching enzymes from non-nematode species. The nucleotide homology of Hg-MMP to any known genes is so low that the BLAST search of more than 1.6 million sequences against the 1880-bp long Hg-MMP sequence did not return any homologous genes with an E-value below 0.1. The singularity of the newly discovered MP from H. glycines and its involvement in hatching will be studied further.