X-ray reflectivity and grazing incidence diffraction studies of interaction between human adhesion/growth-regulatory galectin-1 and DPPE—GM1 lipid monolayer at an air/water interface

Abstract

The specific interaction of ganglioside GM1 with the homodimeric (prototype) endogenous lectin galectin-1 triggers growth regulation in tumor and activated effector T cells. This proven biorelevance directed interest to studying association of the lectin to a model surface, i.e. a 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine/ganglioside GM1 (80 : 20 mol%) monolayer, at a bioeffective concentration. Surface expansion by the lectin insertion was detected at a surface pressure of 20 mN/m. On combining the methods of grazing incidence X-ray diffraction and X-ray reflectivity, a transient decrease in lipid-ordered phase of the monolayer was observed. The measured electron density distribution indicated that galectin-1 is oriented with its long axis in the surface plane, ideal for cis-crosslinking. The data reveal a conspicuous difference to the way the pentameric lectin part of the cholera toxin, another GM1-specific lectin, is bound to the monolayer. They also encourage further efforts to monitor effects of structurally different members of the galectin family such as the functionally antagonistic chimera-type galectin-3.

Influence of protein (human galectin-3) design on aspects of lectin activity

“…Considering the multifunctionality that galectins have intra- and extracellularly, and this with specificity for the cell type (and its special status of activation of differentiation) (Kasai 1997 , 2018 ; García Caballero et al 2020a ), work on more than a few assay systems will have to be done to characterize the role of this aspect of galectin structure reliably. Concerning the interplay with glycan counterreceptors, bottom-up tailoring of test platforms such as membrane-surface-like monolayers or nanoparticles such as glycodendrimersomes has already proven informative (Percec et al 2013 ; Majewski et al 2015 ; Gabius 2017 ; Xiao et al 2018 ).…”

Functional interplay between ganglioside GM1 and cross‐linking galectin‐1 induces axon‐like neuritogenesis via integrin‐based signaling and TRPC5‐dependent Ca2+ influx

“…; Majewski et al . ) and (v) Gal‐1, as lectin, is active in axon regeneration in vitro (Horie et al . ; Kopitz et al .…”

Network Monitoring of Adhesion/Growth‐Regulatory Galectins: Localization of the Five Canonical Chicken Proteins in Embryonic and Maturing Bone and Cartilage and Their Introduction as Histochemical Tools

“…When examining the nature of actually functional binding partners for human galectins, not very many but distinct glycoproteins (e.g., fibronectin, laminin, CD7, or α 5 β 1 ‐integrin) or gangliosides (e.g. GM1) were delineated (Ohannesian et al, ; Pace and Baum ; André et al, ; Sanchez‐Ruderisch et al, ; Ledeen et al, ; Majewski et al, ). Thus, appropriate glycosylation and its mode of presentation will team up for a productive lectin–glycoconjugate interplay (Gabius et al, ).…”