Streptococcus suis serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs
or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The
thioredoxin (Trx) system is a key antioxidant system that contributes adversity adaptation and pathogenicity. SS2 has been
shown to encode putative thioredoxin genes, but the biological roles, coding sequence, and underlying mechanisms remains
uncharacterized. Here, we demonstrated that SSU05_0237-ORF, from a clinical SS2 strain, ZJ081101, encodes a protein
of 104 amino acids with a canonical CGPC active motif and an identity 70–85% similar to the thioredoxin A (TrxA) in
other microorganisms. Recombinant TrxA efficiently catalyzed the thiol-disulfide oxidoreduction of insulin. The deletion
of TrxA led to a significantly slow growth and markedly compromised tolerance of the pathogen to temperature stress,
as well as impaired adhesion ability to pig intestinal epithelial cells (IPEC-J2). However, it was not involved in H2O2
and
paraquat-induced oxidative stress. Compared with the wild-type strain, the ΔTrxA strain was more susceptible to killing by
macrophages through increasing NO production. Treatment with TrxA mutant strain also significantly attenuated cytotoxic
effects on RAW 264.7 cells by inhibiting inflammatory response and apoptosis. Knockdown of pentraxin 3 in RAW 264.7
cells was more vulnerable to phagocytic activity, and TrxA promoted SS2 survival in phagocytic cells depending on pentraxin
3 activity compared with the wild-type strain. Moreover, a co-inoculation experiment in mice revealed that TrxA mutant
strain is far more easily cleared from the body than the wild type strain in the period from 8–24 h, and exhibits significantly
attenuated oxidative stress and liver injury. In summary, we reveal the important role of TrxA in the pathogenesis of SS2.
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Thioredoxin C of Streptococcus suis serotype 2 contributes to virulence by inducing antioxidative stress and inhibiting autophagy via the MSR1/PI3K-Akt-mTOR pathway in macrophages Chunxiao Ji, Yanying Pan, Bocheng Liu, Jianying Liu, Chijun Zhao, Zhuyuan Nie, Simeng Liao, Guangwei Kuang, Xin Wu, Quan Liu, Jie Ning, Yulong Tang, Lihua Fang Veterinary Microbiology.2024; 298: 110263. CrossRef
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Trichoderma atroviride is a common fungus found in various
ecosystems that shows mycoparasitic ability on other fungi.
A novel dsRNA virus was isolated from T. atroviride NFCF377
strain and its molecular features were analyzed. The viral
genome consists of a single segmented double-stranded RNA
and is 9,584 bp in length, with two discontinuous open reading
frames (ORF1 and ORF2). A mycoviral structural protein
and an RNA-dependent RNA polymerase (RdRp) are encoded
by ORF1 and ORF2, respectively, between which is found a
canonical shifty heptameric signal motif (AAAAAAC) followed
by an RNA pseudoknot. Analysis of sequence similarity
and phylogeny showed that it is closely related to members
of the proposed family “Fusagraviridae”, with a highest similarity
to the Trichoderma atroviride mycovirus 1 (TaMV1).
Although the sequence similarity of deduced amino acid to
TaMV1 was evident, sequence deviations were distinctive at
untranslated regions (UTRs) due to the extended size. Thus,
we inferred this dsRNA to be a different strain of Trichoderma
atroviride mycovirus 1 (TaMV1-NFCF377). Electron
microscopy image exhibited an icosahedral viral particle of
40 nm diameter. Virus-cured isogenic isolates were generated
and no differences in growth rate, colony morphology, or
conidia production were observed between virus-infected and
virus-cured strains. However, culture filtrates of TaMV1-
NFCF377-infected strain showed enhanced antifungal activity
against the plant pathogen Rhizoctonia solani but not to
edible mushroom Pleurotus ostreatus. These results suggested
that TaMV1-NFCF377 affected the metabolism of the fungal
host to potentiate antifungal compounds against a plant pathogen,
but this enhanced antifungal activity appeared to be
species-specific.
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