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The efforts made to develop vaccines against Streptococcus suis have failed because of lack of common antigens cross-reactive against different serotypes of this species. The cell wall-anchored proteins can be good vaccine candidates due to their high expression and accessibility to antibodies, among these, a cell-wall protein, DNA-nuclease (SsnA), present in most of the S. suis serotypes and clinical isolates collected from infected pigs, was selected. An experimental challenge against S. suis serotype 2 in a pig model was used to validate the efficacy of recombinant SsnA combined with aluminium hydroxide plus Quil A as adjuvants, previously tested in mice by our research group with good results. In our study, clinical characteristics, bacterial load and spread, haematological and immunological parameters and the antibody response, including the opsonophagocytosis analysis of the sera were evaluated. Moreover the composition of peripheral blood leukocyte populations was studied in infected animals. The results show that the immunization of piglets with rSsnA elicits a significant humoral antibody response. However, the antibody response is not reflected in protection of pigs that are challenged with a virulent strain in our conventional vaccination model. Further studies are necessary to evaluate the use of rSsnA as a vaccine candidate for swine.
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http://dx.doi.org/10.1016/j.cimid.2016.06.001 | DOI Listing |
J Clin Invest
September 2025
Division of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Boston, United States of America.
B-lymphocytes play major adaptive immune roles, producing antibody and driving T-cell responses. However, how immunometabolism networks support B-cell activation and differentiation in response to distinct receptor stimuli remains incompletely understood. To gain insights, we systematically investigated acute primary human B-cell transcriptional, translational and metabolomic responses to B-cell receptor (BCR), Toll-like receptor 9 (TLR9), CD40-ligand (CD40L), interleukin-4 (IL4) or combinations thereof.
View Article and Find Full Text PDFInfect Immun
September 2025
National Contagious Bovine Pleuropneumonia Reference Laboratory, State Key Laboratory for Animal Disease Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Contagious bovine pleuropneumonia (CBPP), caused by subsp. (Mmm), is a devastating cattle disease with high morbidity and mortality, threatening cattle productivity in Sub-Saharan Africa and potentially in parts of Asia. Cross-border livestock trade increases the risk of CBPP introduction or reintroduction.
View Article and Find Full Text PDFArch Pharm Res
September 2025
College of Pharmacy and Medical Research Center, Chungbuk National University, 194-21, Osongsaengmyeong 1-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28160, Republic of Korea.
Atopic dermatitis (AD) is an inflammatory skin disease that produces a variety of inflammatory cytokines and chemokines. Chitinase-3-like protein 1 (CHI3L1, YKL-40) significantly contributes to AD-associated inflammatory response and is highly expressed in patients with AD. Therefore, this study elucidated the effects and potential mechanisms of human YKL-40 antibody on AD-affected skin.
View Article and Find Full Text PDFKidney Int
September 2025
Department of Inflammation and Immunity, Lerner Research Institute, Cleveland, Ohio, USA; Transplant Center, Cleveland Clinic, Cleveland, Ohio, USA. Electronic address:
J Virol
September 2025
National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Feline infectious peritonitis virus (FIPV) can cause an immune-mediated disease that is fatal to felines, but there is a lack of clinically effective protection conferred by vaccines. The methyltransferase (MTase) activity of the coronavirus nonstructural proteins nsp14 and nsp16 affects virulence, but there are no studies on the effect of nsp14 and nsp16 mutations affecting enzyme activity on the virulence of FIPV. In this study, we successfully rescued two mutant strains based on the previous infectious clone QS-79, named FIPV QS-79 dnsp14 and dnsp16, by mutating the MTase active sites of nsp14 (N415) and nsp16 (D129).
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