Production and immune response of recombinant Hsp60 and Hsp70 from the salmon pathogen Piscirickettsia salmonis

Abstract

We have isolated and sequenced the genes encoding the heat shock proteins 60 (Hsp60) and 70 (Hsp70) of the salmon pathogen Piscirickettsia salmonis. The sequence analysis revealed the expected two open reading frames that encode proteins with calculated molecular weights of 60,060 and 70,400. The proteins exhibit a 70-80% homology with other known prokaryotic Hsp60 and Hsp70 sequences. The coding regions have been expressed in E. coli as thioredoxin fusion proteins. Both recombinant proteins were shown to elicit a humoral response when injected intraperitoneally in Atlantic salmon and also conferred protection to fish challenged with P. salmonis. The present data will facilitate further studies on the involvement of heat shock proteins in protective immunity of fish to infection by P. salmonis and their potential use in recombinants vaccines against this intracellular pathogen.

Humoral and cellular immune response to Histophilus somni recombinant heat shock protein 60 kDa in farm animals

“…It has been confirmed that immunisation with homologous Hsp60 protects laboratory animals against experimental challenge with Salmonella enteric serovar Typhi (Paliwal et al 2008;Bansal et al 2010), Helicobacter pylori (Yamaguchi et al 2000;Yamaguchi et al 2003), Histoplasma capsulatum (Gomez et al 1995;Deepe and Gibbons 2002), Legionella pneumophila (Blander and Horwitz 1993;Weeratna et al 1994), Yersinia enterocolitica (Noll and Autenrieth 1996), Chlamydia trachomatis (Rank et al 1995), Paracoccidioides brasiliensis (Soares et al 2008), Piscirickettsia salmonis (Wilhelm et al 2005) and Francisella tularensis (Hartley et al 2004). Because of the broad cross-reactivity of H. somni Hsp60 antibodies (Galli 2009;Bajzert 2013) with Hsp60 of Pasteurella multocida, Escherichia coli and Salmonella Enteritidis, it seems to be an promising candidate to vaccinate farm animals and to induce cross-protection.…”

Identification of potential vaccine target antigens by immunoproteomic analysis of a virulent and a non-virulent strain of the fish pathogen Flavobacterium psychrophilum

“…They were expressed in both the virulent and non-virulent strains of Flavobacterium psychrophilum, and HSPs are known to be important targets of the host immune response in other pathogens (Wilhelm et al 2005). Heat shock proteins are considered molecular chaperones expressed by prokaryotes and eukaryotes that bind polypeptide chains, prevent aggregation, and support protein folding (Bukau & Horwich 1998).…”

“…The combined roles of HSPs as antigens and immunomodulators have led to the suggestion that they might provide an important link between innate and acquired immune responses (Srivastava et al 1998). Recently, it was shown that fish immunized using recombinant HSP 60 and HSP 70 from another salmonid pathogen, Piscirickettsia salmonis, elicited a humoral immune response when intraperitoneally injected in Atlantic salmon Salmo salar, and protection was also conferred to fish challenged with P. salmonis (Wilhelm et al 2005). These findings are interesting and suggest that the HSP proteins identified in this study may provide possible vaccine targets.…”

Co-administration of rIpaB domain of Shigella with rGroEL of S. Typhi enhances the immune responses and protective efficacy against Shigella infection

“…They are potent inducers of the immune system, inducing both innate and adaptive immune responses. 27,28 Many microbial HSPs are reported to be dominant antigens that elicit host immune responses to a variety of pathogens [29][30][31][32][33][34] and act as effective adjuvants. 35 Previously, we developed recombinant (r) Hsp 60 (GroEL) and rHsp70 (DnaK) from Salmonella enterica serovar Typhi, and we reported that these candidate vaccine molecules stimulate both arms of immunity against S. Typhi and S. typhimurium infection in mice.…”