A lysozyme-like protein in the salivary glands of adult Aedes aegypti : functional and biochemical characteristics Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/1g05fg19j

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  • This study investigated some functional and biochemical characteristics of a bacteriolytic protein in the salivary glands of adult Aedes aecupti. A method for the isolation of this protein from other mosquito salivary gland components is also described. Based on some of its biochemical properties, this bacteriolytic protein can be classified as a lysozyme. This protein is strongly-linked to mosquito sugarfeeding activity because there is a statistically significant (P < 0.05) increase in the levels of lytic activity six hours before mosquitoes start to sugar feed. By its bacteriolytic action, it may function as a protective mechanism against bacteria-contaminated sugar meals. Preliminary work suggests that mosquitoes exposed to lyophilized Micrococcus lysodeikticus in their sugar meal respond by increasing the lytic activity in their salivary glands. The levels of bacteriolytic activity are apparently not affected by bloodfeeding. In the absence of feeding, as in teneral and bloodfed mosquitoes, salivary bacteriolytic activity increases to a maximum, then levels off. This suggests a regulation of the synthesis of this salivary protein that is independent of the feeding state of the adult mosquito. A combination of centrifugation, polyacrylamide gel electrophoresis (non-denaturing and denaturing), cation exchange chromatography and gel filtration, was used to isolate the protein from other mosquito salivary gland components. This salivary protein is lysozyme-like in several aspects: 1) it lyses bacterial cell walls of M. lysodeikticus, 2) it is a basic protein with a pI between 7.47 and 8.89, 3) it is thermostable at low pH, and loses its activity at high pH, and 4) it is composed of one polypeptide chain. Its molecular weight is twice that of hen egg white lysozyme. This salivary bacteriolytic protein is the first insect exocrine lysozyme to be characterized.
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