2021
DOI: 10.3390/toxins13070485
|View full text |Cite
|
Sign up to set email alerts
|

Helicobacter pylori BabA–SabA Key Roles in the Adherence Phase: The Synergic Mechanism for Successful Colonization and Disease Development

Abstract: Helicobacter pylori is a pathogenic microorganism that successfully inhabits the human stomach, colonizing it by producing several virulence factors responsible for preventing host self-defense mechanisms. The adherence mechanism to gastric mucosal tissue is one of the most important processes for effective colonization in the stomach. The blood group antigen-binding adhesion (BabA) and sialic acid-binding adherence (SabA) are two H. pylori outer membrane proteins able to interact with antigens in the gastrodu… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
40
0
2

Year Published

2022
2022
2024
2024

Publication Types

Select...
8
2

Relationship

0
10

Authors

Journals

citations
Cited by 43 publications
(43 citation statements)
references
References 69 publications
1
40
0
2
Order By: Relevance
“…The adhesion of H. pylori to lymphocytes may be mediated by the interaction between the bacterium’s own molecules and molecules on the cell surface. H. pylori strain 26695, that was used in this research, contains LacdiNAc domain-binding adhesins (LabA), lipoproteins A and B (AlpA/AlpB), sialic acid-binding adhesin (SabA), blood group antigen-binding adhesin (BabA), and lipopolysaccharide (LPS), which are recognized by mucin 5AC (MUC5AC), laminin, Lex sialic acid (Le x ), Lewis b antigen (Le b ), and Toll like-receptor 4 (TLR4), respectively, which are all present in PBMCs [ 3 , 24 , 25 , 26 , 27 ]. On the other hand, for the first time it is reported that the CagA oncoprotein of H. pylori enters the cytoplasm of PBMCs.…”
Section: Discussionmentioning
confidence: 99%
“…The adhesion of H. pylori to lymphocytes may be mediated by the interaction between the bacterium’s own molecules and molecules on the cell surface. H. pylori strain 26695, that was used in this research, contains LacdiNAc domain-binding adhesins (LabA), lipoproteins A and B (AlpA/AlpB), sialic acid-binding adhesin (SabA), blood group antigen-binding adhesin (BabA), and lipopolysaccharide (LPS), which are recognized by mucin 5AC (MUC5AC), laminin, Lex sialic acid (Le x ), Lewis b antigen (Le b ), and Toll like-receptor 4 (TLR4), respectively, which are all present in PBMCs [ 3 , 24 , 25 , 26 , 27 ]. On the other hand, for the first time it is reported that the CagA oncoprotein of H. pylori enters the cytoplasm of PBMCs.…”
Section: Discussionmentioning
confidence: 99%
“…SabA recognizes Sialyl-Lewis x and sialyl-Lewis antigens expressed on the gastric epithelium [ 115 ]. Both BabA and SabA enables H. pylori to adhere to the gastric mucosa and subsequent colonization [ 116 ].…”
Section: Virulence and Pathogenesis Mechanismsmentioning
confidence: 99%
“…The major activators for NF- κ B and AP-1 by H. pylori are CagA and LPS [ 46 , 47 ]. Adhesion molecules of H. pylori , antigen binding adhesion A (BabA), sialic acid binding adherence A (SabA), or outer membrane protein Q (HopQ), allow attachment of the bacteria to gastric epithelial cells [ 48 ]. LPS binds to TLR4, a member of signal transduction proteins, to induce the expression of transcriptional factors including NF- κ B and AP-1 mostly in macrophages and gastric epithelial cells [ 49 ].…”
Section: H Pylori and Immune Systemmentioning
confidence: 99%