The results from the present study indicate that LvIntegrin could regulate cell proliferation and may have a major role in modulating the efficiency of proliferation factor signaling. LvIntegrin, a shrimp b integrin was identified from L. vannamei, shared several highly conserved features, such as bA domain, hybrid domain and the metal ion-dependent adhesion site. To characterize the immune functions of LvIntegrin, the temporal mRNA expression of LvIntegrin in hemocytes of shrimps challenged with L. anguillarum and the bacterial and fungal agglutination activities of rLvIntegrin were determined. The expression of LvIntegrin in hemocytes was significantly upregulated after L. anguillarum challenge, and in the presence of bivalent cation, rLvIntegrin could significantly agglutinate all the tested bacteria and fungi. The results suggested that LvIntegrin exhibited broad-spectrum agglutination activity towards both bacteria and fungi and served critical, individual roles in cellsubstrate interactions during immune response. The rate of proliferation of NIH3T3 cells showed significant improvement in a dose-dependent manner when they were treated with rLvIntegrin, indicates that LvIntegrin would regulate cell proliferation. Chagas disease, which was once thought to be an exotic disease confined to endemic regions of Latin America, has now gone global becoming a new worldwide challenge. We have reported that the parasite up-regulates the expression of TSP-1 and other extracellular matrix proteins in human coronary artery smooth muscle cells in order to enhance the process of cellular invasion. It has been suggested that T. cruzi trypomastigotes bind to several extracellular matrix components such as laminin, fibronectin, collagen and human galectin-3 to increase cellular infection through not well understood mechanisms. Thrombospondins have been described as “matricellular proteins” because they play a role in OTX015 regulating cellular responses and ECM remodeling in the pericellular microenvironment but they are non-essential components of the mature matrix fibrils. The role of TSP-1 in vitro and in vivo is complex and context specific, because it interacts with a wide array of cellular proteins. TSP-1 is a large homotrimeric glycoprotein containing several domains that can bind to cell surface receptors and extracellular molecules. TSP-1 is composed of several characterized distinct domains including the N-terminal heparin binding domain, procollagen region, type 1, 2 and 3 repeats and a C-terminal domain. The molecule also contains highly conserved Epidermal Growth Factor repeats, type 3 repeats and a C-terminal domain, which includes the signature domain that can interact with integrins and CD47. The C-terminal domain of the thrombospondin family is highly conserved compared to the N-terminal domain, which is different for each thrombospondin isoform. Calreticulin is a major intracellular well conserved calcium-binding chaperone, which was identified in skeletal muscle and is present in the cells of all higher organisms except erythrocytes.