Journal of Microbiology

Journal Article

The cytoplasmic loops of AgrC contribute to the quorum-sensing activity of Staphylococcus aureus: Qian Huang , Yihui Xie , Ziyu Yang , Danhong Cheng , Lei He , Hua Wang , Qian Liu , Min Li; J. Microbiol. 2021;59(1):92-100. Published online November 17, 2020; DOI: https://doi.org/10.1007/s12275-021-0274-x

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In Staphylococcus aureus, the accessory gene regulator (agr) quorum-sensing system is thought to play an important role in biofilm formation. The histidine kinase AgrC is one of the agr system components and activated by the self-generated auto-inducing peptide (AIP), which is released continuously into the extracellular environment during bacterial growth. The extracellular loops (Extra-loops) of AgrC are crucial for AIP binding. Here, we reported that the cytoplasmic loops (Cyto-loops) of AgrC are also involved in Agr activity. We identified S. aureus ST398 clinical isolates containing a naturally occurring single amino acid substitution (lysine to isoleucine) at position 73 of an AgrC Cyto-loop that exhibited significantly stronger biofilm formation and decreased Agr activity compared to the wild-type strain. A constructed strain containing the K73I point mutation in AgrC Cyto-loop continued to show a growth dependent induction of the agr system, although the growth dependent induction was delayed by about 6 h compared to the wild-type. In addition, a series of strains containing deletion mutants of the AgrC Cyto- and Extra-loops were constructed and revealed that the removal of the two Cyto-loops and Extra-loops 2 and 3 totally abolished the Agr activity and the growth-dependence on the agr system induction. Remarkably, the Extra-loop 1 deletion did not affect the Agr activity. In conclusion, the AgrC Cyto-loops play a crucial role in the S. aureus quorum-sensing activity.

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Review

MINIREVIEW] Multilayered regulations of RIG-I in the anti-viral signaling pathway: Nari Kim , Hesung Now , Nhung T.H. Nguyen , Joo-Yeon Yoo; J. Microbiol. 2016;54(9):583-587. Published online August 31, 2016; DOI: https://doi.org/10.1007/s12275-016-6322-2

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Abstract

RIG-I is a cytosolic receptor recognizing virus-specific RNA structures and initiates an antiviral signaling that induces the production of interferons and proinflammatory cytokines. Because inappropriate RIG-I signaling affects either viral clearance or immune toxicity, multiple regulations of RIG-I have been investigated since its discovery as the viral RNA detector. In this review, we describe the recent progress in research on the regulation of RIG-I activity or abundance. Specifically, we focus on the mechanism that modulates RIGI- dependent antiviral response through post-translational modifications of or protein-protein interactions with RIG-I.

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Biochemical Characteristics of a Killer Toxin Produced by Ustilago maydis Virus SH14 Isolated in Korea: Ham Eun Soo , Yie, Se Won , Choi, Hyung Tae; J. Microbiol. 1997;35(4):323-326.

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Abstract: Toxin protein from Ustilago maydis virus SH14 isolated in Korea was purified using ethanol precipitation, cation exchange, gel filtration and anion exchange chromatography. The molecular weight of the purified protein was estimated to be 8.3 kDa by SDS-PAGE analysis. The Nterminal sequence of the protein is L-G-I-N-C(K)-R-G-S-S-Q--C(K)-G-L-S-G which is highly homologous with that of P4 toxin, but the amino acid composition and electrophoretic mobility in a native PAGE of the toxin protein were totally different from those of P4 toxin respectively. The SH14 toxin was shown to have immunological cross-reactivity about 50% with P4 toxin when examined by Western hybridization.

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