Detection and structural mapping of potential fucosyltransferases motif sequences in some insect species

Purpose: Fucosyltransferases (FucTs) catalyze the transfer (fucosylation) of α-L-fucose from GDP-Fuc onto N- and O-linked glycans, free oligosaccharides, or lipids or directly onto proteins. In mammals, 13 fucosyltransferase gene families (FUT) have been identified, including FUT 1-11, POFUT1 (Protein O-fucosyltransferase 1) and POFUT2 (Protein O-fucosyltransferase 2) Despite the existing studies in the literature, the diversity of many fucosyltransferases in organisms remains unknown. In insects, there are few studies on fucosyltransferase and FUT types are not characterized by species. Method: Fucosyltransferase motif sequences were determined from the transcriptomes (all mRNA sequences) obtained from the databases of 5 insects (Bombyx mori, Callosobruchus maculatus, Galleria mellonella, Manduca sexta, Myzus persicae) with known genomes through databases, and putative fucosyltransferase sequences in insects were determined with computational analysis (Clustal Omega, Prosite ve MEME-Suite/FIMO). Then, the similarities between the three-dimensional protein structures of the mammalian fucosyltransferase enzymes were revealed using Swiss-Model, AlphaFold and pyMOL databases.Findings: Based on motif and three-dimensional structure comparison regions, all 13 fucosyltransferases were identified in Callosobruchus maculatus, FucT1 and FucT9 in Galleria mellonella, FucT1, FucT4, FucT5, FucT8, and FucT11 in Manduca sexta, FucT2, FucT3, FucT5, FucT6, FucT7, FucT9, FucT10, and FucT11 in Myzus persicae, and FucT1, FucT3, FucT5, FucT6, and FucT9 motifs were characterized in Bombyx mori.Conclusion: This information provides guidance for continuing studies on fucosyltransferases in invertebrates. New sequences for the fucosyltransferase enzyme will be revealed as the genome of determined insects is studied. While the similarities of fucosyltransferase motifs in insects and mammals indicate that they may be orthologous genes in terms of evolution, it is also an indication that new developmental and evolutionary studies will be conducted on this subject.

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Journal
Biological Diversity and Conservation
Published
2026-05-31
DOI
https://doi.org/10.46309/biodicon.2026.1904444
Primary Topic
Glycosylation and Glycoproteins Research
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article
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article

Detection and structural mapping of potential fucosyltransferases motif sequences in some insect species

Savaş İzzetoğlu, Ceren Ersoy, Gamze Turgay İzzetoğlu, Sadiye Oylum
Biological Diversity and Conservation
Glycosylation and Glycoproteins Research
article

Detection and structural mapping of potential fucosyltransferases motif sequences in some insect species

Savaş İzzetoğlu, Ceren Ersoy, Gamze Turgay İzzetoğlu, Sadiye Oylum
article en

Abstract

Purpose: Fucosyltransferases (FucTs) catalyze the transfer (fucosylation) of α-L-fucose from GDP-Fuc onto N- and O-linked glycans, free oligosaccharides, or lipids or directly onto proteins. In mammals, 13 fucosyltransferase gene families (FUT) have been identified, including FUT 1-11, POFUT1 (Protein O-fucosyltransferase 1) and POFUT2 (Protein O-fucosyltransferase 2) Despite the existing studies in the literature, the diversity of many fucosyltransferases in organisms remains unknown. In insects, there are few studies on fucosyltransferase and FUT types are not characterized by species. Method: Fucosyltransferase motif sequences were determined from the transcriptomes (all mRNA sequences) obtained from the databases of 5 insects (Bombyx mori, Callosobruchus maculatus, Galleria mellonella, Manduca sexta, Myzus persicae) with known genomes through databases, and putative fucosyltransferase sequences in insects were determined with computational analysis (Clustal Omega, Prosite ve MEME-Suite/FIMO). Then, the similarities between the three-dimensional protein structures of the mammalian fucosyltransferase enzymes were revealed using Swiss-Model, AlphaFold and pyMOL databases.Findings: Based on motif and three-dimensional structure comparison regions, all 13 fucosyltransferases were identified in Callosobruchus maculatus, FucT1 and FucT9 in Galleria mellonella, FucT1, FucT4, FucT5, FucT8, and FucT11 in Manduca sexta, FucT2, FucT3, FucT5, FucT6, FucT7, FucT9, FucT10, and FucT11 in Myzus persicae, and FucT1, FucT3, FucT5, FucT6, and FucT9 motifs were characterized in Bombyx mori.Conclusion: This information provides guidance for continuing studies on fucosyltransferases in invertebrates. New sequences for the fucosyltransferase enzyme will be revealed as the genome of determined insects is studied. While the similarities of fucosyltransferase motifs in insects and mammals indicate that they may be orthologous genes in terms of evolution, it is also an indication that new developmental and evolutionary studies will be conducted on this subject.

Biological Diversity and ConservationVol. 19(2)
Ege University (TR)
Openalex Percentile: Top 9%
Glycosylation and Glycoproteins Research
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