The biological role of core 1β1-3galactosyltransferase (T-synthase) in mucin-type O-glycosylation in Silkworm, Bombyx mori

Morio, Akihiro; Lee, Jae Man; Fujii, Tsuguru; Mon, Hiroaki; Masuda, Akihiro; Kakino, Kohei; Xu, Jian; Banno, Yutaka; Kusakabe, Takahiro

doi:10.1016/j.ibmb.2023.103936

Cited by 1 publication

(4 citation statements)

References 37 publications

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“…This has been shown for Caenorhabditis elegans ( Ju et al. 2006 ) and Bombyx mori ( Morio et al. 2023 ).…”

Section: Discussionmentioning

confidence: 58%

“… 2006 ) and Bombyx mori ( Morio et al. 2023 ). In our studies on mollusc T-synthases (from Biomphalaria glabrata , Pomacea canaliculata and Crassostrea gigas ( Zemkollari et al.…”

Section: Discussionmentioning

confidence: 99%

“… 2006 ) or insects ( Drosophila melanogaster and Bombyx mori ) ( Yoshida et al. 2008 ; Morio et al. 2023 ).…”

Section: Discussionmentioning

confidence: 99%

“… 2008 ; Morio et al. 2023 ). However, even this small sample of examples shows clearly, that although when there are some similarities with vertebrates, the glycosylation machinery of invertebrates is much more complex and diverse.…”

Section: Discussionmentioning

confidence: 99%

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Molecular cloning, characterisation and molecular modelling of two novel T-synthases from mollusc origin

Zemkollari,

Oostenbrink,

Grabherr

et al. 2024

Glycobiology

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The glycoprotein-N-acetylgalactosamine β1,3-galactosyltransferase, known as T-synthase (EC 2.4.1.122), plays a crucial role in the synthesis of the T-antigen, which is the core 1 O-glycan structure. This enzyme transfers galactose from UDP-Gal to GalNAc-Ser/Thr. The T-antigen has significant functions in animal development, immune response, and recognition processes. Molluscs are a successful group of animals that inhabit various environments, such as freshwater, marine, and terrestrial habitats. They serve important roles in ecosystems as filter feeders and decomposers but can also be pests in agriculture and intermediate hosts for human and cattle parasites. The identification and characterization of novel carbohydrate active enzymes, such as T-synthase, can aid in the understanding of molluscan glycosylation abilities and their adaptation and survival abilities. Here, the T-synthase enzymes from the snail Pomacea canaliculata and the oyster Crassostrea gigas are identified, cloned, expressed, and characterized, with a focus on structural elucidation. The synthesized enzymes display core 1 β1,3-galactosyltransferase activity using pNP-α-GalNAc as substrate and exhibit similar biochemical parameters as previously characterised T-synthases from other species. While the enzyme from C. gigas shares the same structural parameters with the other enzymes characterised so far, the T-synthase from P. canaliculata lacks the consensus sequence CCSD, which was previously considered indispensable.

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“…This has been shown for Caenorhabditis elegans ( Ju et al. 2006 ) and Bombyx mori ( Morio et al. 2023 ).…”

Section: Discussionmentioning

confidence: 58%

“… 2006 ) and Bombyx mori ( Morio et al. 2023 ). In our studies on mollusc T-synthases (from Biomphalaria glabrata , Pomacea canaliculata and Crassostrea gigas ( Zemkollari et al.…”

Section: Discussionmentioning

confidence: 99%

“… 2006 ) or insects ( Drosophila melanogaster and Bombyx mori ) ( Yoshida et al. 2008 ; Morio et al. 2023 ).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Molecular cloning, characterisation and molecular modelling of two novel T-synthases from mollusc origin

Zemkollari,

Oostenbrink,

Grabherr

et al. 2024

Glycobiology

View full text Add to dashboard Cite

show abstract

The biological role of core 1β1-3galactosyltransferase (T-synthase) in mucin-type O-glycosylation in Silkworm, Bombyx mori

Cited by 1 publication

References 37 publications

Molecular cloning, characterisation and molecular modelling of two novel T-synthases from mollusc origin

Molecular cloning, characterisation and molecular modelling of two novel T-synthases from mollusc origin

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