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- 저자 : Pan Yanying (검색결과 2 건)
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Guochao Shi,Mingli Wang,Yanying Zhu,Xiaoya Yan, Siye Pan,Siye Pan,Anqi Zhang 한국물리학회 2019 Current Applied Physics Vol.19 No.11
An effective SERS-based detection method has been developed to quantitatively diagnose the goat serum which overcomes the problem of diffusion limitation in traditional heterogeneous immunoassay. In this work, the ultrasensitive silver/anodic aluminum oxide (Ag/AAO) SERS platform was explored via magnetron sputtering which can precisely control the sample morphology and intergap distances. Results indicated that the localized surface plasmon resonance (LSPR) effect was sharply strengthened as the sub-10 nm nanogaps generated and the enhancement factor (EF) for crystal violet (CV) was calculated to be 3.677×107. This novel Ag/AAO substrate with substantial “hot spots” exhibited high SERS sensitivity which could obtain extremely low limits of detection (LOD) of 10−12M for CV. Importantly, this SERS platform was employed to detect goat serum and reached a LOD at 1 ng/μl. As a nondestructive detection technique, our SERS-based methodology required small sample quantity which expected to achieve more biomolecular detection.
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Zhao Chijun,Jia Xinglin,Pan Yanying,Liao Simeng,Zhang Shuo,Ji Chunxiao,Kuang Guangwei,Wu Xin,Liu Quan,Tang Yulong,Fang Lihua 한국미생물학회 2023 The journal of microbiology Vol.61 No.4
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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