TY - JOUR
T1 - F-Type Lectins
T2 - A highly diversified family of fucose-binding proteins with a unique sequence motif and structural fold, involved in self/non-self-recognition
AU - Vasta, Gerardo R.
AU - Mario Amzel, L.
AU - Bianchet, Mario A.
AU - Cammarata, Matteo
AU - Feng, Chiguang
AU - Saito, Keiko
N1 - Funding Information:
The author's research reviewed herein was supported by Grants IOS 1050518, IOB-0618409, MCB 0077928, and IOS-0822257 from the National Science Foundation, Grant R01GM070589 from the National Institutes of Health (GV); grant ARRA-1RO1NS061827 from the NIH (LA); and NIGMS pre-doctoral fellowship GM14903-04 from the NIH to Eric W. Odom.
Publisher Copyright:
© 2017 Vasta, Amzel, Bianchet, Cammarata, Feng and Saito.
PY - 2017/11/29
Y1 - 2017/11/29
N2 - The F-type lectin (FTL) family is one of the most recent to be identified and structurally characterized. Members of the FTL family are characterized by a fucose recognition domain [F-type lectin domain (FTLD)] that displays a novel jellyroll fold ("F-type" fold) and unique carbohydrate- and calcium-binding sequence motifs. This novel lectin family comprises widely distributed proteins exhibiting single, double, or greater multiples of the FTLD, either tandemly arrayed or combined with other structurally and functionally distinct domains, yielding lectin subunits of pleiotropic properties even within a single species. Furthermore, the extraordinary variability of FTL sequences (isoforms) that are expressed in a single individual has revealed genetic mechanisms of diversification in ligand recognition that are unique to FTLs. Functions of FTLs in self/non-self-recognition include innate immunity, fertilization, microbial adhesion, and pathogenesis, among others. In addition, although the F-type fold is distinctive for FTLs, a structure-based search revealed apparently unrelated proteins with minor sequence similarity to FTLs that displayed the FTLD fold. In general, the phylogenetic analysis of FTLD sequences from viruses to mammals reveals clades that are consistent with the currently accepted taxonomy of extant species. However, the surprisingly discontinuous distribution of FTLDs within each taxonomic category suggests not only an extensive structural/functional diversification of the FTLs along evolutionary lineages but also that this intriguing lectin family has been subject to frequent gene duplication, secondary loss, lateral transfer, and functional co-option.
AB - The F-type lectin (FTL) family is one of the most recent to be identified and structurally characterized. Members of the FTL family are characterized by a fucose recognition domain [F-type lectin domain (FTLD)] that displays a novel jellyroll fold ("F-type" fold) and unique carbohydrate- and calcium-binding sequence motifs. This novel lectin family comprises widely distributed proteins exhibiting single, double, or greater multiples of the FTLD, either tandemly arrayed or combined with other structurally and functionally distinct domains, yielding lectin subunits of pleiotropic properties even within a single species. Furthermore, the extraordinary variability of FTL sequences (isoforms) that are expressed in a single individual has revealed genetic mechanisms of diversification in ligand recognition that are unique to FTLs. Functions of FTLs in self/non-self-recognition include innate immunity, fertilization, microbial adhesion, and pathogenesis, among others. In addition, although the F-type fold is distinctive for FTLs, a structure-based search revealed apparently unrelated proteins with minor sequence similarity to FTLs that displayed the FTLD fold. In general, the phylogenetic analysis of FTLD sequences from viruses to mammals reveals clades that are consistent with the currently accepted taxonomy of extant species. However, the surprisingly discontinuous distribution of FTLDs within each taxonomic category suggests not only an extensive structural/functional diversification of the FTLs along evolutionary lineages but also that this intriguing lectin family has been subject to frequent gene duplication, secondary loss, lateral transfer, and functional co-option.
KW - F-type lectins
KW - Fucolectins
KW - Fucose-binding
KW - Glycan recognition
KW - Innate immunity
KW - Self/non-self-recognition
KW - Structural modeling
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U2 - 10.3389/fimmu.2017.01648
DO - 10.3389/fimmu.2017.01648
M3 - Review article
C2 - 29238345
AN - SCOPUS:85036563758
VL - 8
JO - Frontiers in Immunology
JF - Frontiers in Immunology
SN - 1664-3224
IS - NOV
M1 - 1648
ER -