Goose-Type Lysozyme Inhibitor (PliG) Enhances Survival of Escherichia coli in Goose Egg Albumen

Vanderkelen, Lise; Herreweghe, J.M. Van; Callewaert, Lien; Michiels, Chris W.

doi:10.1128/aem.00427-11

Cited by 6 publications

(5 citation statements)

References 23 publications

(15 reference statements)

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“…In addition to the novel O-specific polysaccharide biosynthesis genes and other LPS biosynthesis genes, we also identified metabolism, regulatory, and transport genes involved in bacterial resistance to lysozyme. However, the genes for proteinaceous lysozyme inhibitors, such as Ivy [ 13 ], MliC (membrane bound lysozyme inhibitor of c-type lysozyme) [ 14 ], and PliG (periplasmic lysozyme inhibitor of g-type lysozyme) [ 15 , 29 ], were not identified in our screen. The performed deletion and lysozyme inhibition assays indicated that these “other” genes did not appear to play a significant role in the ExPEC resistance to lysozyme in our in vitro model (Yinli Bao, data not shown).…”

Section: Discussionmentioning

confidence: 99%

“…These findings suggest that the true physiological functions of Ivy, MliC, and PliG might be to control excessive activity of endogenous bacterial autolysins, with the inhibition of exogenous lysozyme as a simply fortuitous coincidence. The localization of the proteinaceous inhibitors to the periplasm (MliC is bound to the luminal side of the outer membrane) [ 13-15 , 29 ] rather than to the external milieu further suggests that the O-specific polysaccharide at the bacterial surface may play a much more important role in protecting bacteria against exogenous lysozyme than proteinaceous inhibitors.…”

Section: Discussionmentioning

confidence: 99%

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O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

et al. 2018

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Extraintestinal pathogenic Escherichia coli (ExPEC) is the leading cause of bloodstream and other extraintestinal infections in human and animals. The greatest challenge encountered by ExPEC during an infection is posed by the host defense mechanisms, including lysozyme. ExPEC have developed diverse strategies to overcome this challenge. The aim of this study was to characterize the molecular mechanism of ExPEC resistance to lysozyme. For this, 15,000 transposon mutants of a lysozyme-resistant ExPEC strain NMEC38 were screened; 20 genes were identified as involved in ExPEC resistance to lysozyme—of which five were located in the gene cluster between galF and gnd, and were further confirmed to be involved in O-specific polysaccharide biosynthesis. The O-specific polysaccharide was able to inhibit the hydrolytic activity of lysozyme; it was also required by the complete lipopolysaccharide (LPS)-mediated protection of ExPEC against the bactericidal activity of lysozyme. The O-specific polysaccharide was further shown to be able to directly interact with lysozyme. Furthermore, LPS from ExPEC strains of different O serotypes was also able to inhibit the hydrolytic activity of lysozyme. Because of their cell surface localization and wide distribution in Gram-negative bacteria, O-specific polysaccharides appear to play a long-overlooked role in protecting bacteria against exogenous lysozyme.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

et al. 2018

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“…In support of this hypothesis, Ivy was shown to be essential for the ability of E. coli to grow in human saliva and to enhance its ability to survive in egg white of chicken eggs, both of which contain only c-type lysozyme [10] . PliG, on the other hand, enhanced survival of E. coli in goose egg white, which contains only g-type lysozyme, but not in chicken egg white [11] . These results indicate that a highly specific one-to-one interaction between host lysozymes and bacterial lysozyme inhibitors may affect bacteria-host interactions.…”

Section: Introductionmentioning

confidence: 95%

Role of Lysozyme Inhibitors in the Virulence of Avian Pathogenic Escherichia coli

et al. 2012

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Lysozymes are key effectors of the animal innate immunity system that kill bacteria by hydrolyzing peptidoglycan, their major cell wall constituent. Recently, specific inhibitors of the three major lysozyme families occuring in the animal kingdom (c-, g- and i-type) have been discovered in Gram-negative bacteria, and it has been proposed that these may help bacteria to evade lysozyme mediated lysis during interaction with an animal host. Escherichia coli produces two inhibitors that are specific for c-type lysozyme (Ivy, Inhibitor of vertebrate lysozyme; MliC, membrane bound lysozyme inhibitor of c-type lysozyme), and one specific for g-type lysozyme (PliG, periplasmic lysozyme inhibitor of g-type lysozyme). Here, we investigated the role of these lysozyme inhibitors in virulence of Avian Pathogenic E. coli (APEC) using a serum resistance test and a subcutaneous chicken infection model. Knock-out of mliC caused a strong reduction in serum resistance and in in vivo virulence that could be fully restored by genetic complementation, whereas ivy and pliG could be knocked out without effect on serum resistance and virulence. This is the first in vivo evidence for the involvement of lysozyme inhibitors in bacterial virulence. Remarkably, the virulence of a ivy mliC double knock-out strain was restored to almost wild-type level, and this strain also had a substantial residual periplasmic lysozyme inhibitory activity that was higher than that of the single knock-out strains. This suggests the existence of an additional periplasmic lysozyme inhibitor in this strain, and indicates a regulatory interaction in the expression of the different inhibitors.

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“…The first such inhibitor was discovered in Escherichia coli in 2001 and was named Ivy (inhibitor of vertebrate lysozyme) [7]. Later, several additional inhibitors have been identified in different bacteria, with specificity against c-type [8,9], g-type [10], and i-type lysozymes [11], and there is increasing evidence that these inhibitors contribute to bacterial symbiosis or pathogenesis by allowing evasion of their host's immune defense [12][13][14][15][16]. Several of these inhibitors have been well characterized and show a very high affinity for their cognate lysozymes.…”

Section: Introductionmentioning

confidence: 99%

Lysozyme Inhibitors as Tools for Lysozyme Profiling: Identification and Antibacterial Function of Lysozymes in the Hemolymph of the Blue Mussel

Vanderkelen,

Van Herreweghe,

Michiels

2023

Molecules

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Lysozymes are universal components of the innate immune system of animals that kill bacteria by hydrolyzing their main cell wall polymer, peptidoglycan. Three main families of lysozyme have been identified, designated as chicken (c)-, goose (g)- and invertebrate (i)-type. In response, bacteria have evolved specific protein inhibitors against each of the three lysozyme families. In this study, we developed a serial array of three affinity matrices functionalized with a c-, g-, and i-type inhibitors for lysozyme typing, i.e., to detect and differentiate lysozymes in fluids or extracts from animals. The tool was validated on the blue mussel (Mytilus edulis), whose genome carries multiple putative i-, g-, and c-type lysozyme genes. Hemolymph plasma of the animals was found to contain both i- and g-type, but not c-type lysozyme. Furthermore, hemolymph survival of Aeromonas hydrophila and E. coli strains lacking or overproducing the i- type or g-type lysozyme inhibitor, respectively, was analyzed to study the role of the two lysozymes in innate immunity. The results demonstrated an active role for the g-type lysozyme in the innate immunity of the blue mussel, but failed to show a contribution by the i-type lysozyme. Lysozyme profiling using inhibitor-based affinity chromatography will be a useful novel tool for studying animal innate immunity.

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Goose-Type Lysozyme Inhibitor (PliG) Enhances Survival of Escherichia coli in Goose Egg Albumen

Cited by 6 publications

References 23 publications

O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli

Role of Lysozyme Inhibitors in the Virulence of Avian Pathogenic Escherichia coli

Lysozyme Inhibitors as Tools for Lysozyme Profiling: Identification and Antibacterial Function of Lysozymes in the Hemolymph of the Blue Mussel

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