Bacterial chitinases and chitin-binding proteins as virulence factors

Frederiksen, Rikki F.; Paspaliari, Dafni Katerina; Larsen, Tanja; Storgaard, Birgit G.; Larsen, Mona; Ingmer, Hanne; Palcic, Monica M.; Leisner, Jørgen J.

doi:10.1099/mic.0.051839-0

Cited by 156 publications

(122 citation statements)

References 115 publications

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“…1). One XVIP (XAC2609) has a complete PG-binding domain (residues 219-280) and a region (residues 30-120) with similarity to the catalytic region of proteins of glycoside hydrolase family 19 (GH19) that possess chitinase-or lysozyme-like activities 22 ( Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

Bacterial killing via a type IV secretion system

et al. 2015

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Section: Resultsmentioning

confidence: 99%

Bacterial killing via a type IV secretion system

et al. 2015

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“…It can be perceived, however, that glycans that contain either a LacNAc or LacdiNAc motif might be a part of the target with the concomitant alterations in glycosylation contributing to the pathogenic response. It is of considerable interest that chitinases produced by bacterial pathogens such as Legionella pneumophila, Listeria monocytogenes and Salmonella may act as virulence factors by targeting similar substrates [31]. …”

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confidence: 99%

Human chitotriosidase CHIT1 cross reacts with mammalian‐like substrates

Larsen¹,

Yoshimura²,

Voldborg³

et al. 2014

FEBS Letters

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a b s t r a c tHumans do not synthesize chitin, yet they produce a number of active and inactive chitinases. One of the active enzymes is chitotriosidase whose serum levels are elevated in a number of diseases such as Gaucher's disease and upon fungal infection. Since the biological role of chitotriosidase in disease pathogenesis is not understood we screened a panel of mammalian GlcNAc-containing glycoconjugates as alternate substrates. LacNAc and LacdiNAc-terminating substrates are hydrolyzed, the latter with a turnover comparable to that of pNP-chitotriose. Glycolipids or glycoproteins with LacNAc and LacdiNAc represent potential chitinase substrates and the subsequent alteration of glycosylation pattern could be a factor in disease pathogenesis.

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“…We thus hypothesized that ChiA has other functions besides those associated with vector colonization and transmission. ChiA has been identified as a virulence factor of the bacterial pathogens of vertebrate hosts, which also lack endogenous chitin [33]. In those cases it has been suggested that GlcNAc-containing glycans may be the targets of ChiA, such as N-acetyllactosamine, which is common in vertebrate glycoconjugates [34].…”

Section: Discussionmentioning

confidence: 99%

A chitinase is required for Xylella fastidiosa colonization of its insect and plant hosts

et al. 2017

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Xylella fastidiosa colonizes the xylem network of host plant species as well as the foregut of its required insect vectors to ensure efficient propagation. Disease management strategies remain inefficient due to a limited comprehension of the mechanisms governing both insect and plant colonization. It was previously shown that X. fastidiosa has a functional chitinase (ChiA), and that chitin likely serves as a carbon source for this bacterium. We expand on that research, showing that a chiA mutant strain is unable to grow on chitin as the sole carbon source. Quantitative PCR assays allowed us to detect bacterial cells in the foregut of vectors after pathogen acquisition; populations of the wild-type and complemented mutant strain were both significantly larger than the chiA mutant strain 10 days, but not 3 days, post acquisition. These results indicate that adhesion of the chiA mutant strain to vectors may not be impaired, but that cell multiplication is limited. The mutant was also affected in its transmission by vectors to plants. In addition, the chiA mutant strain was unable to colonize host plants, suggesting that the enzyme has other substrates associated with plant colonization. Lastly, ChiA requires other X. fastidiosa protein(s) for its in vitro chitinolytic activity. The observation that the chiA mutant strain is not able to colonize plants warrants future attention to be paid to the substrates for this enzyme.

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Bacterial chitinases and chitin-binding proteins as virulence factors

Cited by 156 publications

References 115 publications

Bacterial killing via a type IV secretion system

Bacterial killing via a type IV secretion system

Human chitotriosidase CHIT1 cross reacts with mammalian‐like substrates

A chitinase is required for Xylella fastidiosa colonization of its insect and plant hosts

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