Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection
Chlamydia trachomatis (Ct) constitutes the most prevalent sexually transmitted bacterium worldwide. Chlamydial infections can lead to severe clinical sequelae including pelvic inflammatory disease, ectopic pregnancy, and tubal infertility. As an obligate intracellular pathogen, Ct has evolved multip...
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2018
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v115_n26_pE6000_Lujan http://hdl.handle.net/20.500.12110/paper_00278424_v115_n26_pE6000_Lujan |
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paper:paper_00278424_v115_n26_pE6000_Lujan2023-06-08T14:54:34Z Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection Chlamydia trachomatis Galectin-1 Glycosylation Host–pathogen interactions Sexually transmitted diseases bacterial protein cell receptor galectin 1 bacterial protein galectin 1 LGALS1 protein, human animal experiment Article cell interaction chlamydiasis controlled study epithelium cell female female genital system human human cell in vivo study male genital system mouse nonhuman priority journal protein expression protein glycosylation protein protein interaction animal Chlamydia trachomatis genetics HeLa cell line lymphogranuloma venereum male metabolism pathology Animals Bacterial Proteins Chlamydia trachomatis Female Galectin 1 HeLa Cells Humans Lymphogranuloma Venereum Male Mice Chlamydia trachomatis (Ct) constitutes the most prevalent sexually transmitted bacterium worldwide. Chlamydial infections can lead to severe clinical sequelae including pelvic inflammatory disease, ectopic pregnancy, and tubal infertility. As an obligate intracellular pathogen, Ct has evolved multiple strategies to promote adhesion and invasion of host cells, including those involving both bacterial and host glycans. Here, we show that galectin-1 (Gal1), an endogenous lectin widely expressed in female and male genital tracts, promotes Ct infection. Through glycosylation-dependent mechanisms involving recognition of bacterial glycoproteins and N-glycosylated host cell receptors, Gal1 enhanced Ct attachment to cervical epithelial cells. Exposure to Gal1, mainly in its dimeric form, facilitated bacterial entry and increased the number of infected cells by favoring Ct–Ct and Ct–host cell interactions. These effects were substantiated in vivo in mice lacking Gal1 or complex β1–6-branched N-glycans. Thus, disrupting Gal1–N-glycan interactions may limit the severity of chlamydial infection by inhibiting bacterial invasion of host cells. © 2018 National Academy of Sciences. All Rights Reserved. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v115_n26_pE6000_Lujan http://hdl.handle.net/20.500.12110/paper_00278424_v115_n26_pE6000_Lujan |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Chlamydia trachomatis Galectin-1 Glycosylation Host–pathogen interactions Sexually transmitted diseases bacterial protein cell receptor galectin 1 bacterial protein galectin 1 LGALS1 protein, human animal experiment Article cell interaction chlamydiasis controlled study epithelium cell female female genital system human human cell in vivo study male genital system mouse nonhuman priority journal protein expression protein glycosylation protein protein interaction animal Chlamydia trachomatis genetics HeLa cell line lymphogranuloma venereum male metabolism pathology Animals Bacterial Proteins Chlamydia trachomatis Female Galectin 1 HeLa Cells Humans Lymphogranuloma Venereum Male Mice |
| spellingShingle |
Chlamydia trachomatis Galectin-1 Glycosylation Host–pathogen interactions Sexually transmitted diseases bacterial protein cell receptor galectin 1 bacterial protein galectin 1 LGALS1 protein, human animal experiment Article cell interaction chlamydiasis controlled study epithelium cell female female genital system human human cell in vivo study male genital system mouse nonhuman priority journal protein expression protein glycosylation protein protein interaction animal Chlamydia trachomatis genetics HeLa cell line lymphogranuloma venereum male metabolism pathology Animals Bacterial Proteins Chlamydia trachomatis Female Galectin 1 HeLa Cells Humans Lymphogranuloma Venereum Male Mice Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| topic_facet |
Chlamydia trachomatis Galectin-1 Glycosylation Host–pathogen interactions Sexually transmitted diseases bacterial protein cell receptor galectin 1 bacterial protein galectin 1 LGALS1 protein, human animal experiment Article cell interaction chlamydiasis controlled study epithelium cell female female genital system human human cell in vivo study male genital system mouse nonhuman priority journal protein expression protein glycosylation protein protein interaction animal Chlamydia trachomatis genetics HeLa cell line lymphogranuloma venereum male metabolism pathology Animals Bacterial Proteins Chlamydia trachomatis Female Galectin 1 HeLa Cells Humans Lymphogranuloma Venereum Male Mice |
| description |
Chlamydia trachomatis (Ct) constitutes the most prevalent sexually transmitted bacterium worldwide. Chlamydial infections can lead to severe clinical sequelae including pelvic inflammatory disease, ectopic pregnancy, and tubal infertility. As an obligate intracellular pathogen, Ct has evolved multiple strategies to promote adhesion and invasion of host cells, including those involving both bacterial and host glycans. Here, we show that galectin-1 (Gal1), an endogenous lectin widely expressed in female and male genital tracts, promotes Ct infection. Through glycosylation-dependent mechanisms involving recognition of bacterial glycoproteins and N-glycosylated host cell receptors, Gal1 enhanced Ct attachment to cervical epithelial cells. Exposure to Gal1, mainly in its dimeric form, facilitated bacterial entry and increased the number of infected cells by favoring Ct–Ct and Ct–host cell interactions. These effects were substantiated in vivo in mice lacking Gal1 or complex β1–6-branched N-glycans. Thus, disrupting Gal1–N-glycan interactions may limit the severity of chlamydial infection by inhibiting bacterial invasion of host cells. © 2018 National Academy of Sciences. All Rights Reserved. |
| title |
Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| title_short |
Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| title_full |
Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| title_fullStr |
Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| title_full_unstemmed |
Glycosylation-dependent galectin–receptor interactions promote Chlamydia trachomatis infection |
| title_sort |
glycosylation-dependent galectin–receptor interactions promote chlamydia trachomatis infection |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v115_n26_pE6000_Lujan http://hdl.handle.net/20.500.12110/paper_00278424_v115_n26_pE6000_Lujan |
| _version_ |
1768543789682524160 |