Glycosylation with heptose residues mediated by the <i>aah</i> gene product is essential for adherence of the AIDA‐I adhesin

Benz, Inga; Schmidt, M. Alexander

doi:10.1046/j.1365-2958.2001.02487.x

Cited by 163 publications

(205 citation statements)

References 42 publications

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“…The ability to vary protein glycosylation has been described for M. tuberculosis Apa glycoproteins, which show differences in delayed-type hypersensitivity reactions and T-lymphocyte stimulation related to the extent of protein glycosylation (43,44). Other biological roles that carbohydrate modifications on bacterial glycoproteins have been shown to affect include adhesion (45), protection against proteolytic cleavage (46), solubility (47), antigenic variation (48), and protective immunity (49). In C. jejuni, alteration of the N-linked glycosylation pathway by mutation in the pgl locus has already been shown to influence adherence, invasion, colonization, and immunogenicity (3,4).…”

Section: Discussionmentioning

confidence: 99%

Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

Young¹,

Brisson

Kelly

et al. 2002

Journal of Biological Chemistry

397

396

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Section: Discussionmentioning

confidence: 99%

Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

Young¹,

Brisson

Kelly

et al. 2002

Journal of Biological Chemistry

397

396

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“…In addition, glycoproteins play a role in interactions between bacteria and their surroundings. Often, glycoproteins are important virulence factors and antigens involved in adhesion events (e.g., AIDA-I of E. coli 2787 [286]), immune modulation (e.g., Apa glycoprotein of M. tuberculosis [287,288]), and evasion (e.g., the pili of N. meningitidis [66,289,290]). Protein glycosylation is often also heterogeneous and dynamic: one protein can carry more than one type of glycan, and glycans can be incomplete or modified.…”

Section: Protein Glycosylationmentioning

confidence: 99%

“…The AIDA-I adhesin was identified in diarrheagenic E. coli clinical isolate 2787, and its glycosylation was found to be essential for adhesion to human intestinal cells (286). The main role of AIDA-I is thought to lie in the stabilization of the protein at the cell surface, offering protection against the action of the numerous proteases present in the gut (282).…”

Section: Protein Glycosylationmentioning

confidence: 99%

“…As in TibA glycosylation, the heptoses are added to AIDA-I by a heptosyltransferase, Aah (encoded by aidA), immediately upstream of the AIDA-I gene. AIDA-I is modified with up to 19 heptose residues, which come from ADPglycero-manno-heptose precursors from the LPS pathway of E. coli (286). Glycosylation was found to occur at the extracellular domain, which is a ␤-helix and harbors imperfect repeats of 19 amino acids.…”

Section: Protein Glycosylationmentioning

confidence: 99%

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The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

Tytgat

Lebeer

2014

Microbiol Mol Biol Rev

128

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SUMMARY Humans have been increasingly recognized as being superorganisms, living in close contact with a microbiota on all their mucosal surfaces. However, most studies on the human microbiota have focused on gaining comprehensive insights into the composition of the microbiota under different health conditions (e.g., enterotypes), while there is also a need for detailed knowledge of the different molecules that mediate interactions with the host. Glycoconjugates are an interesting class of molecules for detailed studies, as they form a strain-specific barcode on the surface of bacteria, mediating specific interactions with the host. Strikingly, most glycoconjugates are synthesized by similar biosynthesis mechanisms. Bacteria can produce their major glycoconjugates by using a sequential or an en bloc mechanism, with both mechanistic options coexisting in many species for different macromolecules. In this review, these common themes are conceptualized and illustrated for all major classes of known bacterial glycoconjugates, with a special focus on the rather recently emergent field of glycosylated proteins. We describe the biosynthesis and importance of glycoconjugates in both pathogenic and beneficial bacteria and in both Gram-positive and -negative organisms. The focus lies on microorganisms important for human physiology. In addition, the potential for a better knowledge of bacterial glycoconjugates in the emerging field of glycoengineering and other perspectives is discussed.

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“…Besides its role as an adhesin, AIDA-I has been shown to mediate self-association and biofilm formation (14) as well as invasion of epithelial cells (15). Additionally, this protein undergoes a modification that is rare in bacteria, as it is O-glycosylated by the specific cytoplasmic protein autotransporter adhesin heptosyltransferase (Aah) (16,17). AIDA-I has been suggested to be a member of a new group of autotransporter called self-associating autotransporters, which includes the Ag43 aggregation factor and the TibA invasin (18).…”

mentioning

confidence: 99%

Autoprocessing of the Escherichia coli AIDA-I Autotransporter

Charbonneau

Janvore²,

Mourez

2009

Journal of Biological Chemistry

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The cleavage of the autotransporter adhesin involved in diffuse adherence (AIDA-I) of Escherichia coli yields a membraneembedded fragment, AIDAc, and an extracellular fragment, the mature AIDA-I adhesin. The latter remains noncovalently associated with AIDAc but can be released by heat treatment. In this study we determined the mechanism of AIDA-I cleavage. We showed that AIDA-I processing is an autocatalytic event by monitoring the in vitro cleavage of an uncleaved mutant protein isolated from inclusion bodies. Furthermore, by following changes in circular dichroism spectra and protease resistance of the renaturated protein, we showed that the cleavage of the protein is correlated with folding. With site-directed deletions, we showed that the catalytic activity of the protein lies in a region encompassing amino acids between Ala-667 and Thr-953, which includes the conserved junction domain of some autotransporters. With site-directed point mutations, we also found that Asp-878 and Glu-897 are involved in the processing of AIDA-I and that a mutation preserving the acidic side chain of Asp-878 was tolerated, giving evidence that this carboxylic acid group is directly involved in catalysis. Last, we confirmed that cleavage of AIDA-I is intramolecular. Our results unveil a new mechanism of auto-processing in the autotransporter family.Monomeric autotransporters, secreted by the type Va secretion pathway, constitute one of the largest family of secreted proteins in Gram-negative bacteria (1). Various virulence attributes have been associated with most autotransporters, such as adhesion or invasion, self-association, biofilm formation, serum resistance, and cytotoxic activity to name just a few (2, 3). Autotransporters are synthesized as pre-proproteins with modular organizations. An N-terminal sec-dependent signal sequence permits the secretion of the protein across the inner membrane (4). A C-terminal membrane-embedded domain promotes secretion of parts of the protein across the outer membrane and is composed of a ␤-barrel and a ␣-helix spanning its lumen (5, 6). The central domain of the protein is, thus, extracellular and bears its functional part. In some cases the extracellular part of the protein is cleaved and remains associated with the outer membrane or is secreted in the extracellular milieu. Directly preceding the membrane-embedded domain, a functional subdomain of ϳ100 amino acids is sometimes present in the extracellular domain and has been called the junction region (also named autochaperone domain or stable core) (7-9). This region is essential for stabilizing the ␤-barrel and/or to promote folding of the extracellular domain (7-9).The adhesin involved in diffuse adherence (AIDA-I) 3 is a monomeric autotransporter that has been extensively studied. AIDA-I was originally identified as a plasmid-encoded protein from a diffusely adhering Escherichia coli strain isolated in a case of infantile diarrhea (10). This adhesin was then shown to play a role in neonatal and postweaning diarrheal diseases in pigle...

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Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA‐I adhesin

Cited by 163 publications

References 42 publications

Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

Structure of the N-Linked Glycan Present on Multiple Glycoproteins in the Gram-negative Bacterium, Campylobacter jejuni

The Sweet Tooth of Bacteria: Common Themes in Bacterial Glycoconjugates

Autoprocessing of the Escherichia coli AIDA-I Autotransporter

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