A novel multivalent vaccine based on secretary antigen-delivery induces protective immunity against Vibrio anguillarum and Aeromonas hydrophila

Zhou, Lingyun; Wang, Xiuhua; Liu, Qin; Wang, Qiyao; Zhao, Yan; Zhang, Yuanxing

doi:10.1016/j.jbiotec.2009.12.010

Cited by 29 publications

(19 citation statements)

References 28 publications

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“…In this study, tilapia immunized with recombinant GAPDH combined with WC+ISA had a higher survival rate than that of fish immunized with WC+ISA only; in addition, fish immunized with GAPDH+ISA alone also had a rate of 50% RPS. Previous studies using recombinant GAPDH vaccine, including Streptococcus iniae, Aeromonas hydrophila and E. tarda, revealed that combining recombinant GAPDH protein with WC or recombinant protein vaccines provides better protection than only a subunit vaccine or WC vaccine (Ra et al, 2009;Shimmoto et al, 2010;Zhou et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

“…Notably, with exposed epitopes on their cell surface (including fimbriae and porins) OMPs are easily recognized as foreign substances by the immunological defense system of the hosts (Kawai et al, 2004). Moreover, according to several studies, vaccines consisting of immunogenic fractions can induce a higher protection than inactivated whole cell (WC) bacteria in fish (Ra et al, 2009;Zhou et al, 2010) and other vertebrates (Zhang et al, 2007).…”

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confidence: 99%

“…Group A streptococci (which includes S. pyogenes, S. equisimilis, S. agalactiae, S. suis and S. pneumonia) and Staphylococcus aureus, in which a cell-surface GAPDH is involved in the interaction with host cells, and adhered to host cells and ligands (Brassard et al, 2004;Maeda et al, 2004;Pancholi and Fischetti, 1992). In Edwardsiella tarda, Vibrio anguillarum, Streptococcus iniae, Aeromonas hydrophila and Vibrio harveyi, GADPHs can induce a protective immune response in fish (Liu et al, 2005Ra et al, 2009;Zhang et al, 2007;Zhou et al, 2010). According to a recent study, GADPHs of Edwardsiella tarda act as a potential vaccine against E. tarda infection; these GAPDHs also protected Vibrio anguillarum in Japanese flounder .…”

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confidence: 99%

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Immunoprotection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactococcus garvieae against Lactococcosis in tilapia

Tsai

Wang

Cao

et al. 2013

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Immunoprotection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactococcus garvieae against Lactococcosis in tilapia

Tsai

Wang

Cao

et al. 2013

J. Gen. Appl. Microbiol.

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“…Moreover, GAPDH is not the only antigen able to induce humoral and memory responses; it is also expected to act as an adjuvant in the immune response. Previous studies using rGAPDH vaccine have shown that combining rGAPDH protein with WC provides better protection than a subunit vaccine or a WC vaccine alone (Ra et al, 2009;Shimmoto et al, 2010;Zhou et al, 2010). Additionally, in other studies, vaccines against Vibrio infected fish demonstrated that the OMP K (OmpK) fused with GAPDH allowed B and T cells to easily recognize the epitopes, which may be a result of providing a more favorable relative position of the B-cell epitopes with regard to the T helper epitopes, and therefore enhanced the immune response.…”

Section: Discussionmentioning

confidence: 99%

Vaccine efficacy of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Edwardsiella ictaluri against E. tarda in tilapia

Cao¹,

Tsai²,

Yang

et al. 2014

J. Gen. Appl. Microbiol.

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Glyceraldehyde-3-phosphate dehydrogenase (GAP-DH), derived from the outer-membrane protein (OMP) fraction, has been used as a potential candidate for vaccine development. The gene-encoding 37 kDa GAPDH outer membrane protein (OMP) from Edwardsiella ictaluri was amplified using polymerase chain reaction (PCR) and was cloned and expressed in Escherichia coli BL21 (DE3). Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blotting, and nucleotide and amino acid sequencing were used to analyze the expressed antigenic protein and gene encoding this protein. Comparative DNA and protein sequence analysis of GAPDH from E. ictaluri GAPDHs from several Gram-negative bacterial species within the Enterobacteriaceae family revealed that the GAPDHs within this group are highly conserved and share a sequence similarity of 75 100% with E. ictaluri GDPDH. Rabbit antiserum raised against the E. ictaluri recombinant GAPDH (rGAPDH) protein recognized purified GADPH, indicating that it has a strong immunogenicity. Tilapia fish were intraperitoneally immunized with formalin-killed E. ictaluri whole cells, and rGAPDH (30 µg fish 1 ) from E. ictaluri, both of which were emulsified in ISA 763A adjuvant. At 3 months after immunization, fish were challenged with the E. tarda strain to assess vaccine efficacy; the relative percent survival (RPS) values were found to exceed 71.4%. The specific mean antibody titer log 2 level of groups vaccinated with rGAPDH at 3 months was significantly higher than that of non-vaccinated fish (control group). Therefore, this recombinant protein can be considered a multi-purpose candidate vaccine against several pathogenic bacteria.Key words: channel catfish; Edwardsiella ictaluri; enteric septicemia of catfish; glyceraldehyde-3-phosphate dehydrogenase (GAPDH) IntroductionEnteric septicemia of catfish (ESC), caused by the bacterial pathogen Edwardsiella ictaluri, was first identified in channel catfish (Ictalurus punctatus) by Hawke (1979). E. ictaluri has become the most lethal infectious disease of channel catfish and other ictalurids in the USA (Plumb, 1999). More than 50% of American catfish fry/fingerling losses are due to ESC (Williams and Lawrence, 2010). E. ictaluri was also isolated from cultured fish species in Indonesia, Vietnam, Japan, Turkey (Crumlish et al., 2002;Keskün et al., 2004;Nagai et al., 2008; Yuas et al., 2003) and China (Ye et al., 2009). ESC is currently controlled using antibiotics; however, extensive use of antimicrobial com pounds reduces their effectiveness by increasing the number of antibiotic-resistant bacterial strains, resulting in the need for higher dosages for effective treatment as well as higher residual amounts of drugs in the harvested fish Thompson and Adams, 2004). Vaccines that protect fish against bacterial diseases are an important alternative to antibiotics and are a safer strategy for disease prevention. Most vaccines for controlling ESC have been tested using Full Paper Vaccine efficacy of glyceraldehyde-3-phosphate dehydrogenase (G...

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“…Our work has been focused on antigen display and secretion systems in the attenuated pathogen Vibrio anguillarum (15,67). Recently we have concentrated our efforts on establishing a bacterial delivery system in which the vector bacteria could produce a large amount of intracellular antigen in vitro, and after being administrated into a host, the resulting strain would lyse efficiently in response to a specific in vivo signal to implement antigen release and biological containment.…”

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confidence: 99%

Iron-Regulated Lysis of Recombinant Escherichia coli in Host Releases Protective Antigen and Confers Biological Containment

Guan

Champeimont

et al. 2011

Infect Immun

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The use of a recombinant bacterial vector vaccine is an attractive vaccination strategy to induce an immune response to a carried protective antigen. The superiorities of live bacterial vectors include mimicry of a natural infection, intrinsic adjuvant properties, and the potential for administration by mucosal routes. Escherichia coli is a simple and efficient vector system for production of exogenous proteins. In addition, many strains are nonpathogenic and avirulent, making it a good candidate for use in recombinant vaccine design. In this study, we screened 23 different iron-regulated promoters in an E. coli BL21(DE3) vector and found one, P viuB , with characteristics suitable for our use. We fused P viuB with lysis gene E, establishing an in vivo inducible lysis circuit. The resulting in vivo lysis circuit was introduced into a strain also carrying an IPTG (isopropyl-␤-Dthiogalactopyranoside)-inducible P T7 -controlled protein synthesis circuit, forming a novel E. coli-based protein delivery system. The recombinant E. coli produced a large amount of antigen in vitro and could deliver the antigen into zebrafish after vaccination via injection. The strain subsequently lysed in response to the iron-limiting signal in vivo, implementing antigen release and biological containment. The gapA gene, encoding the protective antigen GAPDH (glyceraldehyde-3-phosphate dehydrogenase) from the fish pathogen Aeromonas hydrophila LSA34, was introduced into the E. coli-based protein delivery system, and the resultant recombinant vector vaccine was evaluated in turbot (Scophtalmus maximus). Over 80% of the vaccinated fish survived challenge with A. hydrophila LSA34, suggesting that the E. coli-based antigen delivery system has great potential in bacterial vector vaccine applications.

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A novel multivalent vaccine based on secretary antigen-delivery induces protective immunity against Vibrio anguillarum and Aeromonas hydrophila

Cited by 29 publications

References 28 publications

Immunoprotection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactococcus garvieae against Lactococcosis in tilapia

Immunoprotection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Lactococcus garvieae against Lactococcosis in tilapia

Vaccine efficacy of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Edwardsiella ictaluri against E. tarda in tilapia

Iron-Regulated Lysis of Recombinant Escherichia coli in Host Releases Protective Antigen and Confers Biological Containment

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