Evidence for serine protease inhibitor activity in the ovarian calyx fluid of the endoparasitoid Venturia canescens.
نویسندگان
چکیده
Endoparasitic wasps are able to develop inside permissive host insects due to their ability to overcome or evade the host's immune system. In the present study, we provide experimental evidence that ovarian calyx fluid of the ichneumonid endoparasitoid Venturia canescens has the potential to alter host haemocyte spreading and inhibit host haemolymph melanisation due to the presence of a putative serine protease inhibitor (serpin) activity. The existance of a serpin-like activity in the calyx fluid is also supported by experiments where the synthetic protease inhibitor p-APMSF had effects on cellular and cell-free immune reactions similar to ovarian calyx fluid. In addition, based on proteolytic digestion patterns of a wasp egg surface protein, we predict an Arg-specific trypsin-like protease activity in the host haemolymph which is possibly affected by calyx fluid components as well. Our data suggest that ovarian calyx fluid, deposited into the host together with the parasitoid egg, contains serpin activity which might transiently inactivate host defence reactions until other means of protection are established on the egg surface.
منابع مشابه
P 144: Sunflower Mannose binding Lectin-Associated Serine Protease Inhibitor-1 (SFMI-1) and -2: Significant Inhibitors of Mannose binding Lectin Pathway which Helps in Multiple Sclerosis Treatment
One of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. The four pattern recognition molecules that have been identified till now are Mannose binding lectin (MBL), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. MBL ...
متن کاملSerine protease and ovarian paracrine factors in regulation of ovulation.
The controlled target extracellular matrix (ECM) degradation generated by serine protease and regulated by serine protease inhibitor and ovarian paracrine/autocrine factors is an event that affects a wide variety of physiological and pathological processes in the ovary. Evidence cumulated in the past decade clearly showed that the hormone-induced coordinated expression of the tissue-type PA (tP...
متن کاملCloning and Enhanced Expression of an Extracellular Alkaline Protease from a Soil Isolate of Bacillus clausii in Bacillus subtilis
in the detergent industry. In this study, the extracellular alkaline serine protease gene, aprE, from Bacillusclausii was amplified by PCR and further cloned and expressed in B. subtilis WB600 using the pWB980 expression vector. Protease activity of the recombinant B. subtilis WB600 harboring the plasmid pWB980/aprEreached up to 1020 U/ml, approximately 3-folds higher than the nativ...
متن کاملOptimization of Parameters that Affect the Activity of the Alkaline Protease from Halotolerant Bacterium, Bacillus acquimaris VITP4, by the Application of Response Surface Methodology and Evaluation of the Storage Stability of the Enzyme
Background: It was previously shown that the activity of a serine protease from a moderately halotolerant Bacillus aquimaris VITP4 strain is active in a wide range of pH and temperatures and could be modulated by the presence of the divalent metal ions. Objectives: In the present study, a quantitative analysis was done in order to explore the parameters that are contributing to the protease a...
متن کاملThe Effect of TiO2-Nanoparticle on the Activity and Stability of Trypsin in Aqueous Medium
Trypsin (E.C.3.4.21.4) is a serine protease commonly used in proteomics for digestion of proteins. In the present study, the effect of nano-TiO2 on the conformation and catalytic activity of trypsin were studied. The thermal denaturation of trypsin has been investigated in the presence and absence of nano-TiO2 over the temperature range (293-373 K) at pH 3.0 and 7.25, using temperature scanning...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of insect physiology
دوره 46 9 شماره
صفحات -
تاریخ انتشار 2000