Microbe–Host Interactions are Positively and Negatively Regulated by Galectin–Glycan Interactions

Abstract

Microbe–host interactions are complex processes that are directly and indirectly regulated by a variety of factors, including microbe presentation of specific molecular signatures on the microbial surface, as well as host cell presentation of receptors that recognize these pathogen signatures. Cell surface glycans are one important class of microbial signatures that are recognized by a variety of host cell lectins. Host cell lectins that recognize microbial glycans include members of the galectin family of lectins that recognize specific glycan ligands on viruses, bacteria, fungi, and parasites. In this review, we will discuss the ways that the interactions of microbial glycans with host cell galectins positively and negatively regulate pathogen attachment, invasion, and survival, as well as regulate host responses that mitigate microbial pathogenesis.

The galectin lattice at a glance

“…Gal3 promotes raft endocytosis of CD44 and integrins (Furtak et al, 2001;Lakshminarayan et al, 2014), as well as Mgat5-dependent parvovirus internalization and infection (Garcin et al, 2015). Indeed, host galectins recognize microbial glycans and might play a role in pathogen attachment and invasion by viruses, bacteria, fungi and parasites (Baum et al, 2014).…”

The Cek1‑mediated MAP kinase pathway regulates exposure of α‑1,2 and β‑1,2‑mannosides in the cell wall ofCandida albicansmodulating immune recognition

“…Although they are able to stimulate host defense, by directly or indirectly triggering leucocyte activation, phagocytosis, complement fixation and cytokine production, they can act as a bridge to target cells, promoting microbial infection (reviewed in 80 ). In this study we show no significant differences regarding the dendritic cells and macrophage-mediated killing of cek1 or wild type strains between immune cells derived from either galectin-3 C/C or galectin-3 ¡/-mice.…”

N-Glycopeptide Profiling in Arabidopsis Inflorescence

“…Asn-285 displayed two glycoforms, bearing either a single GlcNAc or Man 5 . Asn-316 was represented with four glycoforms, bearing GlcNAc 1-2 , Man 5 , and a complex glycan, GlcNAc 3 Man 3 Hex. Asn-59 and 154 from calreticulin 1 (AT1G56340.1) were detected modified with 12 and 8 different glycoforms, respectively.…”

“…However, there are tissue-and kingdom-specific differences in the Golgi processing (3). The modifications' functions have been best characterized in mammalian species, where in addition to being important in controlling protein folding in the ER, they are involved in cell adhesion (4), cell-cell recognition, including host-pathogen recognition in immune response (5), and regulation of cellular signaling through modification of ligand receptors (6,7). Glycosylation affects protein solubility, stability, and activity, and as the majority of protein therapeutics are glycoproteins, there is a lot of pharmaceutical interest in characterizing glycosylation patterns on recombinant proteins (8).…”