Effect of SXWS/WSXWS peptides on chemotaxis and adhesion of the macrophage‐like cell line J774

Abstract

WSXWS motif is a conserved amino acid sequence which is present in type I cytokine receptors. This motif that can be found both in the ligand binding chains and signal transducer molecule of the receptors with different amino acids at the position 'X', plays a role in the receptor folding, ligand binding and signal transduction as well. Structural analysis proved that WSEWS motif of IL-6R is located in a highly accessible location in the protein.Structural properties and chemotaxis of a tetrapeptide library with SXWS sequence, where X was the 19 proteinogenic amino acids except cystein were systematically studied earlier. It has been proved that C-terminal amidation and the identity of amino acid 'X' had a pronounced influence on the chemotactic properties, but less of the structure of the peptides. Here we present our findings on the effect of a tetra-and a pentapeptide library with the sequence of SXWS and WSXWS on the chemotaxis and adhesion of J774 murine macrophage cell line. We studied the effect of the presence/absence of N-terminal tryptophan and the different amino acids at the 'X' position on these physiological responses. Results indicated that amino acid 'X' had a marked influence on chemotaxis, adhesion as well as on proliferation induced by (W)SXWS peptides. Elongation of SXWS sequence with a tryptophan at the N terminus also altered pronouncedly all the physiological responses of the cells studied. A good correlation could be observed between the chemotaxis and the proliferation and physicochemical parameters of the amino acid 'X'.2

The Role of the PFNA Operon of Bifidobacteria in the Recognition of Host’s Immune Signals: Prospects for the Use of the FN3 Protein in the Treatment of COVID-19

“…One of the distinctive features of type I cytokine receptors is the type III fibronectin domain containing a WS-WS consensus motif (WS-motif, cytokine receptor motif, any amino acid in the middle of the motif) [72]. This motif plays a role in receptor folding, cytokine binding and signal transduction [73]. The results of computer modeling suggest that the region of interaction between interleukins and type I cytokine receptors is adjacent to the WS-WS motif [74].…”

Study of the binding of ΔFN3.1 fragments of the Bifidobacterium longum GT15 with TNFα and prevalence of domain-containing proteins in groups of bacteria of the human gut microbiota

“…FN3 domains have been found in various eukaryotic extracellular and intracellular protein families, including extracellular matrix molecules, enzymes, muscle tissue proteins, and cell surface receptors [including motifs of cytokine receptors (MCRs)] [5,6] . FN3 domains often contain the consensus motif WSXWS (WS motif; MCR; random amino acid in the middle of the motif) [7,8] . This motif plays a role in receptor folding, ligand (cytokine) binding, and signal transduction [9,10] .…”

“…This motif plays a role in receptor folding, ligand (cytokine) binding, and signal transduction [9,10] . Mutations in this motif alter the receptor's ability to bind cytokines [8] . In bacteria, FN3 domains are found in proteins with different enzymatic functions: cellulases [11,12] , hydrolases [1,13] , chitinases [14,15] , and proteases [16] .…”

Ciliary Generation of a Peptidergic Sexual Signal

“…Mass spectrometric analysis of mating ciliary ectosomes led to the identification of an amidated peptide, derived from Cre03.g204500, that acts as a chemotactic modulator, attracting minus gametes while repelling plus gametes (Luxmi et al, 2019). Amidated peptides from echinoderms, Hydra, vespids and humans have also been reported to induce chemotaxis (Palma, 2006;Rowe and Elphick, 2012;Szabó et al, 2015;Takahashi et al, 1997). Cre03.g204500 encodes a 93-kDa protein with all of the features expected of a prepropeptide (hereafter referred to as preproGATI) (Luxmi et al, 2019).…”