The incidence of diseases caused by nontuberculous mycobacteria (NTM) is increasing
annually worldwide, including Japan.
Mycobacterium avium
subsp.
hoiminissuis
(MAH) is one of the most common NTM species responsible
for chronic lung diseases in animals and humans. In the current study, mycobacterial
interspersed repetitive unit-variable number tandem repeat (MIRU-VNTR) typing was employed
to characterize the genetic diversity of swine MAH isolates from Kyushu, Japan. In total,
309 isolates were obtained from the lymph nodes of 107 pigs not displaying any clinical
signs of disease, of which 307 were identified as MAH, comprising 173 strains. Based on
eight established MIRU-VNTR loci, the MAH strains represented 50 genotypes constituting
three lineages, and 29 had not been described in the Mac French National Institute for
Agricultural Research Nouzilly MIRU-VNTR (Mac-INMV) database. MAH was the dominant
M. avium
complex (MAC) in pigs from Kyushu, and there was high genetic
diversity among genotype profiles of MAH from Kyushu. We identified three predominant
genotype profiles in the tested area sharing high relatedness with genotype profiles of
strains isolated in European countries. MAH was the most common NTM in pigs from Kyushu
and exhibited high diversity, with new strain-derived genotypes.
Antibodies that recognized either Babesia gibsoni or canine red blood cell (RBC) 70-kilodalton (kDa) protein were detected in serum from acutely and chronically B. gibsoni-infected. In those sera, antibodies that reacted with recombinant B. gibsoni and canine heat shock protein 70 (rBgHsp70 and rcHsp70) were detected; therefore, B. gibsoni and canine RBC 70-kDa proteins seemed to be BgHsp70 and cHsp70, respectively. In infected dogs, the amounts of these antibodies increased after infection. Interestingly, polyclonal antibody raised against rBgHsp70 in two rabbits reacted not only with rBgHsp70 but also with rcHsp70 and native cHsp70 from canine RBCs. Because BgHsp70 showed high homology with cHsp70 (70.8%), anti-rBgHsp70 antibody might cross-react with cHsp70. Additionally, the localizations of both BgHsp70 and cHsp70 were observed by indirect fluorescence assay. As a result, cHsp70 was not found on the membrane surface of erythrocytes, suggesting that erythrocytes would not be targets of anti-cHsp70 antibody. Meanwhile, only exoerythrocytic parasites were stained by anti-rBgHsp70 antibody. This result showed that BgHsp70 would be expressed on the surface of parasites during the exoerythrocytic stage. These results indicated that BgHsp70 was a highly immunogenic protein in canine B. gibsoni infection, and that exoerythrocytic parasites might be targets of anti-BgHsp70 antibody.
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