Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand Binding

López-Lucendo, María; Solı́s, Dolores; André, Sabine; Hirabayashi, Jun; Kasai, Ken‐ichi; Kaltner, Herbert; Gabius, Hans‐Joachim; Romero, Antonio

doi:10.1016/j.jmb.2004.08.078

Cited by 276 publications

(321 citation statements)

References 73 publications

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“…The ''jelly-roll'' structure of galectin-1 is highly conserved among vertebrates (13)(14)(15)(16)43). Residues crucial for sugar binding, growth inhibition, and dimerization were subject to strict purifying selection during vertebrate evolution: (i) eight residues in the carbohydrate recognition domain are identical in 31 taxa with only conservative replacements for Val-59 and Arg-73 in three species; thus, both the ability and specificity of galectin-1 to bind sugars have been maintained; (ii) sitedirected mutagenesis have shown that Asp-27-Phe-31 are crucial for the growth inhibitory function (44).…”

Section: Highly Conserved Structure and Functional Domains Of Galectimentioning

confidence: 99%

“…Despite the purifying selection acting on galectin-1, evidence for adaptive evolution for key residues was found on the stem of placental mammals. The disjunct codon S-ϾS change at position 62 emphasizes the importance of this residue in sugar binding, as Ser-62 forms H-bonds with Arg-111 to maintain the architecture of the carbohydrate recognition domain (43). The conservative L-ϾI change at position 128 suggests constraint on the hydrophobic nature of the dimerization interface (45).…”

Section: Highly Conserved Structure and Functional Domains Of Galectimentioning

confidence: 99%

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Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal–fetal immune tolerance

Than

Romero²,

Erez³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Galectin-1 is an anti-inflammatory lectin with pleiotropic regulatory functions at the crossroads of innate and adaptive immunity. It is expressed in immune privileged sites and is implicated in establishing maternal-fetal immune tolerance, which is essential for successful pregnancy in eutherian mammals. Here, we show conserved placental localization of galectin-1 in primates and its predominant expression in maternal decidua. Phylogenetic footprinting and shadowing unveil conserved cis motifs, including an estrogen responsive element in the 5 promoter of LGALS1, that were gained during the emergence of placental mammals and could account for sex steroid regulation of LGALS1 expression, thus providing additional evidence for the role of galectin-1 in immuneendocrine cross-talk. Maximum parsimony and maximum likelihood analyses of 27 publicly available vertebrate and seven newly sequenced primate LGALS1 coding sequences reveal that intense purifying selection has been acting on residues in the carbohydrate recognition domain and dimerization interface that are involved in immune functions. Parsimony-and codon model-based phylogenetic analysis of coding sequences show that amino acid replacements occurred in early mammalian evolution on key residues, including gain of cysteines, which regulate immune functions by redox status-mediated conformational changes that disable sugar binding and dimerization, and that the acquired immunoregulatory functions of galectin-1 then became highly conserved in eutherian lineages, suggesting the emergence of hormonal and redox regulation of galectin-1 in placental mammals may be implicated in maternal-fetal immune tolerance.decidua ͉ estrogen ͉ glycocode ͉ immune-endocrine cross-talk ͉ pregnancy T he success of mammalian pregnancy, in which the developing fetus and mother exchange nutrients, gases, and other molecules via the chorioallantoic placenta, requires maternal immune tolerance to fetal allo-antigens (1-4). This tolerance presumably prevents the occurrence of exaggerated inflammation at the implantation site and reduces the danger of destructive immune attacks on the fetus, a danger that the first mammals with an invasive placenta would have faced (5, 6). It seems likely that mechanisms for immune tolerance to invasive placentation were already functioning in the early placental mammals and that immunoregulatory molecules, which had existed before the mammalian placenta evolved, were incorporated in this tolerance and have undergone evolutionary modifications coincident with the emergence of the mammalian placenta. Here, we present evidence that such modifications occurred in a key immunoregulatory molecule, galectin-1.Molecules that have been implicated in conferring maternalfetal immune tolerance include galectin-1, B7 proteins, Crry, Fas ligand, HLA-G, indoleamine 2,3-dioxygenase, and killer cell immunoglobulin-like receptors (2-4, 7-11). These proteins are involved in pathways regulating adaptive or innate immune responses at the maternal-fetal interface, and their di...

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Section: Highly Conserved Structure and Functional Domains Of Galectimentioning

confidence: 99%

Section: Highly Conserved Structure and Functional Domains Of Galectimentioning

confidence: 99%

Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal–fetal immune tolerance

Than

Romero²,

Erez³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…The CBS can be schematically described as having five subsites (A-E) with subsites C and D defining the conserved core b-galactoside-binding site 16 . Human GAL1 exists as a dimer in solution 17 and the presence of more than one CRD in a GAL1 homodimer makes it well suited for mediating cell adhesion, eliciting signalling and forming lattices 7,14 .…”

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confidence: 99%

Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

et al. 2015

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Galectins are glycan-binding proteins involved in various biological processes including cell/cell interactions. During B-cell development, bone marrow stromal cells secreting galectin-1 (GAL1) constitute a specific niche for pre-BII cells. Besides binding glycans, GAL1 is also a pre-B cell receptor (pre-BCR) ligand that induces receptor clustering, the first checkpoint of B-cell differentiation. The GAL1/pre-BCR interaction is the first example of a GAL1/unglycosylated protein interaction in the extracellular compartment. Here we show that GAL1/pre-BCR interaction modifies GAL1/glycan affinity and particularly inhibits binding to LacNAc containing epitopes. GAL1/pre-BCR interaction induces local conformational changes in the GAL1 carbohydrate-binding site generating a reduction in GAL1/glycan affinity. This fine tuning of GAL1/glycan interactions may be a strategic mechanism for allowing pre-BCR clustering and pre-BII cells departure from their niche. Altogether, our data suggest a novel mechanism for a cell to modify the equilibrium of the GAL1/glycan lattice involving GAL1/unglycosylated protein interactions.

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“…This lectin belongs to the prototype group, and forms a homodimer in solution via hydrophobic interactions and hydrogen bonds (López-Lucendo et al, 2004). Glycopeptide 2 was immobilized on Fig.…”

Section: Detection Of H-gal-1 On Sam-5mentioning

confidence: 99%

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

Maljaars

Souza

Halkes

et al. 2008

Biosensors and Bioelectronics

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a b s t r a c tThe development of a biosensor based on surface plasmon resonance is described for the detection of carbohydrate-binding proteins in solution on a Biacore 2000 instrument, using immobilized glycopeptides as ligands. Their selection was based on previous screenings of solid-phase glycopeptide libraries with Ricinus communis agglutinin (RCA 120 ) and human adhesion/growth-regulatory galectin-1 (h-Gal-1). Glycopeptides were immobilized on Au sensor chips functionalized with mixed self-assembled monolayers of different ratios of 11-mercapto-1-undecanol and 11-mercaptoundecanoic acid, and of 3-mercapto-1-propanol and 11-mercaptoundecanoic acid. The biosensors were optimized for the detection of RCA 120 , and a detection limit of 0.13 nM was obtained. Subsequent experiments with h-Gal-1 indicated a detection limit of at least 0.9 nM for this lectin. Additionally, the effect of interfering proteins on the sensitivity of the optimized biosensor was investigated.

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Growth-regulatory Human Galectin-1: Crystallographic Characterisation of the Structural Changes Induced by Single-site Mutations and their Impact on the Thermodynamics of Ligand Binding

Cited by 276 publications

References 73 publications

Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal–fetal immune tolerance

Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal–fetal immune tolerance

Pre-B cell receptor binding to galectin-1 modifies galectin-1/carbohydrate affinity to modulate specific galectin-1/glycan lattice interactions

The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors

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