Streptococcal infections cause significant mortality and high economic losses in the fish farm industry worldwide, including in the culture of golden pompano Trachinotus ovatus L., a species gaining popularity in China. A total of 9 streptococcal strains were isolated from cage-cultured diseased golden pompano in Beihai, Zhanjing, and Shenzhen, China, between 2012 and 2014. Conventional and rapid identification systems were used to determine that the isolates were Streptococcus agalactiae, S. iniae, and S. dysgalactiae subsp. dysgalactiae. All isolates were gram-positive cocci cells in pairs or short-chain, non-motile, catalase negative, α or β hemolytic cocci. The results of multiplex PCR assays and 16S rRNA BLAST analysis also showed that the β hemolytic strains were S. agalactiae and S. iniae and the α hemolytic strain was S. dysgalactiae subsp. dysgalactiae, respectively. Pathogenicity assays revealed that S. agalactiae (lethal dose [LD50]: 6.38 × 10(4) CFU ml(-1)) was more virulent for golden pompano than S. iniae (LD50: 1.47 × 10(7) CFU ml(-1)) and S. dysgalactiae subsp. dysgalactiae (LD50: 2.57 × 10(6) CFU ml(-1)) when they were challenged by intraperiotoneal (i.p.) injection. The results of antibiotic susceptibility showed that all strains were extremely susceptible to cefradine, erythromycin, and cefotaxime but resistant to gentamicin, penicillin G, novobiocin, neomycin, ciprofloxacin, roxithromycin, furazolidone, enrofloxacin, norfloxacin, kanamycin, ampicillin, tetracycline, and vancomycin This is the first report of a phenomenon of golden pompano coinfection with S. agalactiae and S. iniae, which will contribute to the diagnosis and prevention of streptococcicosis.

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Serum amyloid P component (SAP), an ancient short pentraxin of the pentraxin family, plays an essential role in resistance to bacterial infection. In this study, the expression and functional characterization of SAP (OnSAP) in Nile tilapia (Oreochromis niloticus), a primary vertebrate, are investigated. The open reading frame of OnSAP is 645 bp of a nucleotide sequence encoding a polypeptide of 214 amino acids. As a calcium-binding protein, the structure and relative motif of OnSAP is highly similar to those of humans, containing amino acid residues Asn, Glu, Gln and Asp. In healthy fish, OnSAP mRNA is extensively distributed in all eleven tissues examined, with the highest level in spleen. The mRNA expression of OnSAP was significantly up-regulated after being challenged with gram-positive bacterium Streptococcus agalactiae and gram-negative bacterium Aeromonas hydrophila in vivo. In addition, recombinant OnSAP ((r)OnSAP) protein had capacities of binding S. agalactiae or A. hydrophila in the presence of Ca2+. Further, (r)OnSAP helped monocytes/macrophages to efficiently phagocytize bacteria. Moreover, the (r)OnSAP was able to enhance the complement-mediated lysis of the chicken red blood cells. Collectively, the evidence of SAP in tilapia, based on the results including its evolutionary conserved protein structure, bacterial binding and agglutination, opsonophagocytosis of macrophage and hemolysis enhancement, enriches a better understanding of the biological functions of the pentraxin family.

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