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Human galectin-1 and galectin-3 promote Tropheryma whipplei infection
- Source :
- Gut microbes, Gut microbes, Taylor & Francis, 2021, 13 (1), ⟨10.1080/19490976.2021.1884515⟩, Gut microbes, 2021, 13 (1), pp.1884515. ⟨10.1080/19490976.2021.1884515⟩, Gut microbes, Taylor & Francis, 2021, 13 (1), pp.1884515. ⟨10.1080/19490976.2021.1884515⟩, Gut Microbes, Vol 13, Iss 1 (2021), Gut microbes, 2021, 13 (1), ⟨10.1080/19490976.2021.1884515⟩, Gut Microbes, article-version (VoR) Version of Record
- Publication Year :
- 2021
- Publisher :
- HAL CCSD, 2021.
-
Abstract
- Tropheryma whipplei, is an actinobacterium that causes different infections in humans, including Whipple’s disease. The bacterium infects and replicates in macrophages, leading to a Th2-biased immune response. Previous studies have shown that T. whipplei harbors complex surface glycoproteins with evidence of sialylation. However, the exact contribution of these glycoproteins for infection and survival remains obscure. To address this, we characterized the bacterial glycoprofile and evaluated the involvement of human β-galactoside-binding lectins, Galectin-1 (Gal-1) and Galectin-3 (Gal-3) which are highly expressed by macrophages as receptors for bacterial glycans. Tropheryma whipplei glycoproteins harbor different sugars including glucose, mannose, fucose, β-galactose and sialic acid. Mass spectrometry identification revealed that these glycoproteins were membrane- and virulence-associated glycoproteins. Most of these glycoproteins are highly sialylated and N-glycosylated while some of them are rich in poly-N-acetyllactosamine (Poly-LAcNAc) and bind Gal-1 and Gal-3. In vitro, T. whipplei modulates the expression and cellular distribution of Gal-1 and Gal-3. Although both galectins promote T. whipplei infection by enhancing bacterial cell entry, only Gal-3 is required for optimal bacterial uptake. Finally, we found that serum levels of Gal-1 and Gal-3 were altered in patients with T. whipplei infections as compared to healthy individuals, suggesting that galectins are also involved in vivo. Among T. whipplei membrane-associated proteins, poly-LacNAc rich-glycoproteins promote infection through interaction with galectins. T. whipplei modulates the expression of Gal-1 and Gal-3 both in vitro and in vivo. Drugs interfering with galectin–glycan interactions may provide new avenues for the treatment and diagnosis of T. whipplei infections.
- Subjects :
- tropheryma whipplei
Galectin 1
glycosylation
Galectins
Tropheryma
macrophage
RC799-869
Bacterial Proteins
[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system
[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases
galectin-3
Humans
galectin-1
[SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology
ComputingMilieux_MISCELLANEOUS
Glycoproteins
[SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases
Virulence
Macrophages
Polysaccharides, Bacterial
Galactose
Blood Proteins
Diseases of the digestive system. Gastroenterology
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
infection
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
glycans
Whipple Disease
Research Article
Research Paper
Subjects
Details
- Language :
- English
- ISSN :
- 19490976 and 19490984
- Database :
- OpenAIRE
- Journal :
- Gut microbes, Gut microbes, Taylor & Francis, 2021, 13 (1), ⟨10.1080/19490976.2021.1884515⟩, Gut microbes, 2021, 13 (1), pp.1884515. ⟨10.1080/19490976.2021.1884515⟩, Gut microbes, Taylor & Francis, 2021, 13 (1), pp.1884515. ⟨10.1080/19490976.2021.1884515⟩, Gut Microbes, Vol 13, Iss 1 (2021), Gut microbes, 2021, 13 (1), ⟨10.1080/19490976.2021.1884515⟩, Gut Microbes, article-version (VoR) Version of Record
- Accession number :
- edsair.pmid.dedup....f39dfa18139e93cc99be465c2210da9a