Tyrosine sulfation in N-terminal domain of human C5a receptor is necessary for binding of chemotaxis inhibitory protein of Staphylococcus aureus

Liu, Zhen-jia; Yang, Yan; Jiang, Lei; Xu, Yingchun; Wang, Aixia; Du, Guanhua; Gao, Jinming

doi:10.1038/aps.2011.53

Cited by 11 publications

(7 citation statements)

References 37 publications

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“…Thus, C5aR targeting by PVL provides a rationale for the species specificity associated with its lytic activity (199,200). C5aR also serves as a receptor for the chemotaxis-inhibitory protein of S. aureus (CHIPS), which binds to the receptor and prevents neutrophil activation and recruitment (246)(247)(248)(249)(250)(251). Indeed, CHIPS is capable of blocking the PVL interaction with C5aR on host cells (199).…”

Section: Leucocidin Cellular Receptors Dictate Cell and Species Specimentioning

confidence: 99%

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Alonzo

Torres

2014

Microbiol Mol Biol Rev

236

290

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SUMMARY The ability to produce water-soluble proteins with the capacity to oligomerize and form pores within cellular lipid bilayers is a trait conserved among nearly all forms of life, including humans, single-celled eukaryotes, and numerous bacterial species. In bacteria, some of the most notable pore-forming molecules are protein toxins that interact with mammalian cell membranes to promote lysis, deliver effectors, and modulate cellular homeostasis. Of the bacterial species capable of producing pore-forming toxic molecules, the Gram-positive pathogen Staphylococcus aureus is one of the most notorious. S. aureus can produce seven different pore-forming protein toxins, all of which are believed to play a unique role in promoting the ability of the organism to cause disease in humans and other mammals. The most diverse of these pore-forming toxins, in terms of both functional activity and global representation within S. aureus clinical isolates, are the bicomponent leucocidins. From the first description of their activity on host immune cells over 100 years ago to the detailed investigations of their biochemical function today, the leucocidins remain at the forefront of S. aureus pathogenesis research initiatives. Study of their mode of action is of immediate interest in the realm of therapeutic agent design as well as for studies of bacterial pathogenesis. This review provides an updated perspective on our understanding of the S. aureus leucocidins and their function, specificity, and potential as therapeutic targets.

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Section: Leucocidin Cellular Receptors Dictate Cell and Species Specimentioning

confidence: 99%

The Bicomponent Pore-Forming Leucocidins of Staphylococcus aureus

Alonzo

Torres

2014

Microbiol Mol Biol Rev

236

290

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“…The whole protein from the lung was prepared as previously described, with modifications (31). The lungs were harvested and homogenized in lysis buffer containing a protease inhibitor mixture (Sigma-Aldrich).…”

Section: Western Blottingmentioning

confidence: 99%

IRAK-M Associates with Susceptibility to Adult-Onset Asthma and Promotes Chronic Airway Inflammation

Liu

Zhang

Lou

et al. 2019

The Journal of Immunology

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IL-1R-associated kinase (IRAK)-M regulates lung immunity during asthmatic airway inflammation. However, the regulatory effect of IRAK-M differs when airway inflammation persists. A positive association between IRAK-M polymorphisms with childhood asthma has been reported. In this study, we investigated the role of IRAK-M in the susceptibility to adult-onset asthma and in chronic airway inflammation using an animal model. Through genetic analysis of IRAK-M polymorphisms in a cohort of adult-onset asthma patients of Chinese Han ethnicity, we identified two IRAK-M single nucleotide polymorphisms, rs1624395 and rs1370128, genetically associated with adult-onset asthma. Functionally, the top-associated rs1624395, with an enhanced affinity to the transcription factor c-Jun, was associated with a higher expression of IRAK-M mRNA in blood monocytes. In contrast to the protective effect of IRAK-M in acute asthmatic inflammation, we found a provoking impact of IRAK-M on chronic asthmatic inflammation. Following chronic OVA stimulation, IRAK-M knockout (KO) mice presented with significantly less inflammatory cells, a lower Th2 cytokine level, a higher IFN-g concentration, and increased percentage of Th1 cells in the lung tissue than wild type mice. Moreover, lung dendritic cells (DC) from OVA-treated IRAK-M KO mice expressed a higher percentage of costimulatory molecules PD-L1 and PD-L2. Mechanistically, in vitro TLR ligation led to a greater IFN-g production by IRAK-M KO DCs than wild type DCs. These findings demonstrated a distinctive role of IRAK-M in maintaining chronic Th2 airway inflammation via inhibiting the DC-mediated Th1 activation and indicated a complex role for IRAK-M in the initiation and progression of experimental allergic asthma.

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“…There are three tyrosine residues at the N terminus of C5a 1 receptor, two of which (Tyr11, Tyr14) are proximal to Asp residues, making them potential sulfation sites (Rosenquist and Nicholas, 1993). Both Tyr11 and Tyr14 are sulfated, and this modification is essential for the binding of C5a (Farzan et al, 2001), C5a des-Arg , and CHIPS (Ippel et al, 2009;Liu et al, 2011c).…”

Section: A Introductionmentioning

confidence: 99%

“…The C5a 1 receptor mutations Y14F and Y11F induced a 50% reduction or complete loss of binding affinity for C5a, respectively, indicating the importance of these sulfations in the formation of the N-terminal binding site (Farzan et al, 2001). The binding of CHIPS, which acts as an antagonist for the C5a 1 receptor, has also been shown to be dependent on the sulfation of tyrosine residues 11 and 14 (Ippel et al, 2009;Liu et al, 2011c) (Section IV.C.2).…”

Section: A Introductionmentioning

confidence: 99%