Sweet receptors mediate the adhesion of the gastric pathogen<i>Helicobacter pylori</i>: glycoproteomic strategies

Magalhães, Ana; Ismail, Mohd Nazri; Reis, Celso A.

doi:10.1586/epr.10.18

Cited by 19 publications

(14 citation statements)

References 25 publications

(25 reference statements)

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“…The antigen-binding adhesin BabA binds to fucosylated antigens normally expressed by secretor individuals 212 , and the sialic acid-binding adhesin SabA recognizes sialylated Lewis glycans (sialyl Lewis a (SLe a ) and SLe x ) expressed in gastritis 213 . Inflammation-induced glycosylation alterations, such as the aberrant overexpression of SLe x , occur because of changes in glycosyltransferases expression 59,60,214 . Changes in glycosylation have also been studied in acute-phase proteins, such as α1 antitrypsin, as potential biomarkers in cancer and in acute and chronic inflammatory conditions 215 .…”

Section: Box 3 | Glycosylation At the Interface Of Inflammation-inducmentioning

confidence: 99%

Glycosylation in cancer: mechanisms and clinical implications

2015

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Despite recent progress in understanding the cancer genome, there is still a relative delay in understanding the full aspects of the glycome and glycoproteome of cancer. Glycobiology has been instrumental in relevant discoveries in various biological and medical fields, and has contributed to the deciphering of several human diseases. Glycans are involved in fundamental molecular and cell biology processes occurring in cancer, such as cell signalling and communication, tumour cell dissociation and invasion, cell-matrix interactions, tumour angiogenesis, immune modulation and metastasis formation. The roles of glycans in cancer have been highlighted by the fact that alterations in glycosylation regulate the development and progression of cancer, serving as important biomarkers and providing a set of specific targets for therapeutic intervention. This Review discusses the role of glycans in fundamental mechanisms controlling cancer development and progression, and their applications in oncology.

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Section: Box 3 | Glycosylation At the Interface Of Inflammation-inducmentioning

confidence: 99%

Glycosylation in cancer: mechanisms and clinical implications

2015

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“…Typical oligosaccharide structures of human clusterin. On the basis of Cabezas‐Cruz & de la Fuente (2017) and Magalhães, Ismail, & Reis (2010). Fuc, fucose; Gal, galactose; GlcNAc, n ‐acetylglucosamine; SA, sialic acid…”

Section: The Role Of Clu Glycosylationmentioning

confidence: 99%

Could the glycosylation analysis of seminal plasma clusterin become a novel male infertility biomarker?

Janiszewska¹,

Kratz²

2020

Molecular Reproduction Devel

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Male infertility is becoming a rapidly growing problem around the world, mainly in the highly developed countries. Seminal proteome composition seems to be one of the crucial factors of the proper course of fertilizationclusterin (CLU) is among the most important ones. CLU, as one of the crucial seminal plasma glycoproteins, plays a very important role in sperm capacitation and immune tolerance in the female reproductive tract. CLU is also known as a sensitive marker of oxidative stress. It has six N-glycosylation sites and also exhibits chaperone activity. An analysis of changes in the profile and degree of CLU glycosylation may shed some new light on the molecular mechanisms of the fertilization process and may be used as an additional diagnostic marker of male fertility. This study constitutes a review of the recently available literature concerning human seminal CLU, including changes in its glycosylation, analyzed in the context of human reproduction. K E Y W O R D S clusterin, male fertility, semen quality, seminal clusterin glycosylation

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“…Bacterial attachment is mediated by outer membrane adhesins that bind to glycoconjugates present in the gastric mucus layer and lining the surface epithelium of the gastric mucosa [7]. The blood group antigen binding adhesin (BabA) recognizes ABO(H)/Lewis b blood group antigens expressed in glycoproteins from the gastro-intestinal tract by secretor individuals [8–10], whereas the sialic acid binding adhesin (SabA) mediates bacterial attachment through binding to α2,3-sialylated structures, such as sialyl-Lewis a (sialyl-Le a ) and sialyl-Lewis x (sialyl-Le x ) carried by glycosphingolipids and glycoproteins [11].…”

Section: Introductionmentioning

confidence: 99%

Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways

Magalhães

Marcos-Pinto

Nairn

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Helicobacter pylori exploits host glycoconjugates to colonize the gastric niche. Infection can persist for decades promoting chronic inflammation, and in a subset of individuals lesions can silently progress to cancer. This study shows that H. pylori chronic infection and gastric tissue inflammation result in a remodeling of the gastric glycophenotype with increased expression of sialyl-Lewis a/x antigens due to transcriptional up-regulation of the B3GNT5, B3GALT5, and FUT3 genes. We observed that H. pylori infected individuals present a marked gastric local proinflammatory signature with significantly higher TNF-α levels and demonstrated that TNF-induced activation of the NF-kappaB pathway results in B3GNT5 transcriptional up-regulation. Furthermore, we show that this gastric glycosylation shift, characterized by increased sialylation patterns, favors SabA-mediated H. pylori attachment to human inflamed gastric mucosa. This study provides novel clinically relevant insights into the regulatory mechanisms underlying H. pylori modulation of host glycosylation machinery, and phenotypic alterations crucial for life-long infection. Moreover, the biosynthetic pathways here identified as responsible for gastric mucosa increased sialylation, in response to H. pylori infection, can be exploited as drug targets for hindering bacteria adhesion and counteract the infection chronicity.

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Sweet receptors mediate the adhesion of the gastric pathogenHelicobacter pylori: glycoproteomic strategies

Cited by 19 publications

References 25 publications

Glycosylation in cancer: mechanisms and clinical implications

Glycosylation in cancer: mechanisms and clinical implications

Could the glycosylation analysis of seminal plasma clusterin become a novel male infertility biomarker?

Helicobacter pylori chronic infection and mucosal inflammation switches the human gastric glycosylation pathways

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