Identification and Characterization of a Novel Prokaryotic Peptide

Sun, Guogui; Yu, Xiang; Bao, Celimuge; Wang, Lei; Li, Meng; Gan, Jianhua; Qu, Di; Ma, Jinbiao; Chen, Li

doi:10.1074/jbc.m114.605493

Cited by 33 publications

(42 citation statements)

References 31 publications

(19 reference statements)

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“…176 The optimal condition for PNGase F-α is similar to that of PNGase F. Surprisingly, PNGase F is more active to native IgG than denatured IgG, which is opposite to most proteins. 176 It is also found that IgG-Fab, partially bearing N-linked oligosaccharides in the variable regions, is sometimes resistant to PNGase F digestion even though it does not contain α1,3linked fucose residues. 94 These phenomena may result from the inappropriate denaturation of IgG (including non-denatured treatment).…”

Section: Ms/ms For Glycopeptidesmentioning

confidence: 94%

“…PNGase F is insensitive toward the N ‐glycans with core fucose residues with α1,3 linkage . A new PNGase named PNGase F‐α, also identified from Elizabethkingia meningoseptica , is proposed to release α1‐3 core‐fucosylated oligosaccharides . The optimal condition for PNGase F‐α is similar to that of PNGase F. Surprisingly, PNGase F is more active to native IgG than denatured IgG, which is opposite to most proteins .…”

Section: Oligosaccharidesmentioning

confidence: 99%

“…A new PNGase named PNGase F‐α, also identified from Elizabethkingia meningoseptica , is proposed to release α1‐3 core‐fucosylated oligosaccharides . The optimal condition for PNGase F‐α is similar to that of PNGase F. Surprisingly, PNGase F is more active to native IgG than denatured IgG, which is opposite to most proteins . It is also found that IgG‐Fab, partially bearing N ‐linked oligosaccharides in the variable regions, is sometimes resistant to PNGase F digestion even though it does not contain α1,3‐linked fucose residues .…”

Section: Oligosaccharidesmentioning

confidence: 99%

“…38 It is able to hydrolyze a broad spectrum of N-linked glycans from glycopeptides (tripeptides or longer) and glycoproteins. 175,176 It is worth mentioning that the optimal condition for the enzymatic activity of PNGase F is weakly alkaline which may effectively inhibit the dissociation of sialic acid residues during the | 661 digestion process. Compared to PNGase A, PNGase F has higher deglycosylation activity for sialoglycans.…”

Section: Ms/ms For Glycopeptidesmentioning

confidence: 99%

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Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging. The present review is focused on the application of MS related methodologies to the study of both N- and O-linked sialoglycans. We reviewed MS-based strategies for characterizing sialylation by analyzing intact glycoproteins, proteolytic digested glycopeptides, and released glycans. The review concludes with future perspectives in the field.

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Section: Ms/ms For Glycopeptidesmentioning

confidence: 94%

Section: Oligosaccharidesmentioning

confidence: 99%

Section: Oligosaccharidesmentioning

confidence: 99%

Section: Ms/ms For Glycopeptidesmentioning

confidence: 99%

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Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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“…Both types of enzymes are produced as precursors that undergo intramolecular autoproteolysis to produce the mature active proteins (26,27), but PNGases require the presence of more than 2 amino acid residues in the substrate (28), whereas glycosylasparaginases act only in asparagine-oligosaccharides containing 1 amino acid (29). Currently, bacterial PNGases have been characterized only from the human pathogens Elizabethkingia meningoseptica and Elizabethkingia miricola (30,31) and from the soil bacterium Terriglobus roseus (32). In E. meningoseptica, a glycosylasparaginase has also been characterized (33,34).…”

mentioning

confidence: 99%

Unique Microbial Catabolic Pathway for the Human Core N -Glycan Constituent Fucosyl-α-1,6- N -Acetylglucosamine-Asparagine

Becerra

Rodrı́guez-Dı́az

Gozalbo-Rovira

et al. 2020

mBio

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The survival of commensal bacteria in the human gut partially depends on their ability to metabolize host-derived molecules. The use of the glycosidic moiety of N-glycoproteins by bacteria has been reported, but the role of N-glycopeptides or glycoamino acids as the substrates for bacterial growth has not been evaluated. We have identified in Lactobacillus casei strain BL23 a gene cluster (alf-2) involved in the catabolism of the glycoamino acid fucosyl-α-1,6-N-GlcNAc-Asn (6′FN-Asn), a constituent of the core-fucosylated structures of mammalian N-glycoproteins. The cluster consists of the genes alfHC, encoding a major facilitator superfamily (MFS) permease and the α-l-fucosidase AlfC, and the divergently oriented asdA (aspartate 4-decarboxylase), alfR2 (transcriptional regulator), pepV (peptidase), asnA2 (glycosyl-asparaginase), and sugK (sugar kinase) genes. Knockout mutants showed that alfH, alfC, asdA, asnA2, and sugK are necessary for efficient 6′FN-Asn utilization. The alf-2 genes are induced by 6′FN-Asn, but not by its glycan moiety, via the AlfR2 regulator. The constitutive expression of alf-2 genes in an alfR2 strain allowed the metabolism of a variety of 6′-fucosyl-glycans. However, GlcNAc-Asn did not support growth in this mutant background, indicating that the presence of a 6′-fucose moiety is crucial for substrate transport via AlfH. Within bacteria, 6′FN-Asn is defucosylated by AlfC, generating GlcNAc-Asn. This glycoamino acid is processed by the glycosylasparaginase AsnA2. GlcNAc-Asn hydrolysis generates aspartate and GlcNAc, which is used as a fermentable source by L. casei. These data establish the existence in a commensal bacterial species of an exclusive metabolic pathway likely to scavenge human milk and mucosal fucosylated N-glycopeptides in the gastrointestinal tract. IMPORTANCE The gastrointestinal tract accommodates more than 1014 microorganisms that have an enormous impact on human health. The mechanisms enabling commensal bacteria and administered probiotics to colonize the gut remain largely unknown. The ability to utilize host-derived carbon and energy resources available at the mucosal surfaces may provide these bacteria with a competitive advantage in the gut. Here, we have identified in the commensal species Lactobacillus casei a novel metabolic pathway for the utilization of the glycoamino acid fucosyl-α-1,6-N-GlcNAc-Asn, which is present in the core-fucosylated N-glycoproteins from mammalians. These results give insight into the molecular interactions between the host and commensal/probiotic bacteria and may help to devise new strategies to restore gut microbiota homeostasis in diseases associated with dysbiotic microbiota.

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