Clostridium difficile TxAC314 and SLP-36kDa enhance the immune response toward a co-administered antigen.
This study evaluated the in vivo adjuvant activity of two peptides derived from Clostridium difficile: a fragment of the receptor-binding domain of toxin A (TxA(C314)) and a fragment of the 36 kDa surface-layer protein (SLP-36kDa) from strain C253. Their ability to affect the magnitude, distribution and polarization of the immune response against fibronectin-binding protein A (FnbpA), a protective vaccine antigen against Staphylococcus aureus, was evaluated using two different routes of immunization: intranasal and subcutaneous. It was shown that (i) the route of immunization affected the magnitude of the immune response; (ii) both peptides enhanced the production of circulating anti-FnbpA IgG and IgA; (iii) following mucosal immunization TxA(C314) was more effective than SLP-36kDa at inducing antibody in the gastrointestinal tract; (iv) the adjuvant influenced the Th1/Th2 balance; and (v) TxA(C314) was more effective than SLP-36kDa in inducing a cell-mediated response. These studies provide insight into the ability of different C. difficile-derived peptides to differentially affect and polarize the activity of the immune system and on their potential use as adjuvants in newly developed vaccines.
Brun
Paola
P
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
Scarpa
Melania
M
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
Grillo
Alessia
A
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
Palù
Giorgio
G
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
Mengoli
Carlo
C
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
Zecconi
Alfonso
A
Department of Animal Pathology, Hygiene and Health, University of Milan, Milan, Italy.
Spigaglia
Patrizia
P
Department of Infectious, Parasitic and Immune-mediated Diseases, Istituto Superiore di Sanità, Rome, Italy.
Mastrantonio
Paola
P
Department of Infectious, Parasitic and Immune-mediated Diseases, Istituto Superiore di Sanità, Rome, Italy.
Castagliuolo
Ignazio
I
Department of Histology, Microbiology and Medical Biotechnologies, University of Padua, Padua, Italy.
D018829:Adhesins, Bacterial / Q000008:administration & dosage / Q000276:immunology*; D000276:Adjuvants, Immunologic / Q000008:administration & dosage; D000818:Animals; D000907:Antibodies, Bacterial / Q000096:biosynthesis* / Q000097:blood; D001426:Bacterial Proteins / Q000008:administration & dosage / Q000276:immunology*; D001427:Bacterial Toxins / Q000008:administration & dosage / Q000276:immunology*; D001428:Bacterial Vaccines / Q000008:administration & dosage / Q000276:immunology*; D016360:Clostridioides difficile / Q000276:immunology*; D004768:Enterotoxins / Q000008:administration & dosage / Q000276:immunology*; D007070:Immunoglobulin A / Q000096:biosynthesis / Q000097:blood; D007074:Immunoglobulin G / Q000096:biosynthesis / Q000097:blood; D008297:Male; D008562:Membrane Glycoproteins / Q000276:immunology / Q000502:physiology; D051379:Mice; D008807:Mice, Inbred BALB C; D014614:Vaccines, Synthetic / Q000008:administration & dosage / Q000276:immunology
D018829:Adhesins, Bacterial; D000276:Adjuvants, Immunologic; D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D001428:Bacterial Vaccines; D004768:Enterotoxins; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D008562:Membrane Glycoproteins; C055764:S-layer proteins; D014614:Vaccines, Synthetic; C078635:fibronectin-binding proteins, bacterial; C041348:tcdA protein, Clostridium difficile