Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme

Kyomuhendo, Peter; Nilsen, Inge W.; Brandsdal, Bjørn Olav; Smalås, Arne O.

doi:10.1007/s00894-008-0317-9

Cited by 13 publications

(8 citation statements)

References 43 publications

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“…Vanderkelen et al found that PliG could inhibit the activity of gLYZ from goose, salmon and larvacean [47]. The different effect of PliG on MGgLYZ1 and MGgLYZ2 might be ascribed to negative electrostatic environment in the entire substrate binding crevice and different electrostatic surface properties in their three-dimensional structure [48].…”

Section: Discussionmentioning

confidence: 99%

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

Wang¹,

Zhang²,

Zhao

et al. 2012

PLoS ONE

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Two goose-type lysozymes (designated as MGgLYZ1 and MGgLYZ2) were identified from the mussel Mytilus galloprovincialis. MGgLYZ1 mRNA was widely expressed in the examined tissues and responded sensitively to bacterial challenge in hemocytes, while MGgLYZ2 mRNA was predominately expressed and performed its functions in hepatopancreas. However, immunolocalization analysis showed that both these lysozymes were expressed in all examined tissues with the exception of adductor muscle. Recombinant MGgLYZ1 and MGgLYZ2 could inhibit the growth of several Gram-positive and Gram-negative bacteria, and they both showed the highest activity against Pseudomonas putida with the minimum inhibitory concentration (MIC) of 0.95–1.91 µM and 1.20–2.40 µM, respectively. Protein sequences analysis revealed that MGgLYZ2 had lower isoelectric point and less protease cutting sites than MGgLYZ1. Recombinant MGgLYZ2 exhibited relative high activity at acidic pH of 4–5, while MGgLYZ1 have an optimum pH of 6. These results indicated MGgLYZ2 adapted to acidic environment and perhaps play an important role in digestion. Genomic structure analysis suggested that both MGgLYZ1 and MGgLYZ2 genes are composed of six exons with same length and five introns, indicating these genes were conserved and might originate from gene duplication during the evolution. Selection pressure analysis showed that MGgLYZ1 was under nearly neutral selection while MGgLYZ2 evolved under positive selection pressure with three positively selected amino acid residues (Y102, L200 and S202) detected in the mature peptide. All these findings suggested MGgLYZ2 perhaps served as a digestive lysozyme under positive selection pressure during the evolution while MGgLYZ1 was mainly involved in innate immune responses.

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Section: Discussionmentioning

confidence: 99%

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

Wang¹,

Zhang²,

Zhao

et al. 2012

PLoS ONE

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“…Thus, the finding that (i) the production of Ivyc and its homologs is limited to Gram-negative bacteria rather than to Gram-positive bacteria, which possess exposed peptidoglycan and (ii) they are localized to the periplasm rather than to the external milieu was considered a paradox (10). Compounding this paradox is the fact that the Ivyc-like proteins have limited specificity, and they are weak inhibitors of only a subset of the G-type lysozymes (10,17). Furthermore, despite its similarity, Ivyp2, which is produced by some pseudomonads, does not inhibit any type of lysozyme, and its function remained unknown (10).…”

Section: Discussionmentioning

confidence: 99%

“…2 and, perhaps not unexpectedly, the proteins are organized generally according to phylogeny of the producing bacteria. Each member of the Ivyc/p1 family is characterized by the CKPHDC consensus sequence, which has been demonstrated to be essential for binding to C-type lysozymes (10,17). The Ivyp2 paralogs, represented by P. aeruginosa Ivyp2 as the prototype, lack this consensus sequence but possess instead the consensus motif CEXXDXC.…”

Section: Identification and Phylogenetic Analysis Of Ivy Homologs Andmentioning

confidence: 99%

The Vertebrate Lysozyme Inhibitor Ivy Functions to Inhibit the Activity of Lytic Transglycosylase

Clarke¹,

Scheurwater²,

Clarke

2010

Journal of Biological Chemistry

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The proteinaceous inhibitor of vertebrate lysozymes (Ivy) is produced by a collection of Gram-negative bacteria as a stress response to damage to their essential cell wall component peptidoglycan. A paralog of Ivy, Ivyp2 is produced exclusively by a number of pseudomonads, including Pseudomonas aeruginosa, but this protein does not inhibit the lysozymes, and its function was unknown. In this study, we demonstrate that the production of Ivy (homologs of both Ivyp1 and Ivyp2) correlates with bacteria that do not O-acetylate their peptidoglycan, a modification that controls the activity of the lytic transglycosylases. Furthermore, we show that both Ivy proteins are potent inhibitors of the lytic transglycoslyases, enzymes involved in the biosynthesis and maintenance of peptidoglycan. These data suggest that the true physiological function of the Ivy proteins is to control the autolytic activity of lytic transglycosylases within the periplasm of Gram-negative bacteria that do not produce O-acetylated peptidoglycan and that the inhibition of exogenous lysozyme by Ivy is simply a fortuitous coincidence.The cell envelope represents the only major structural element in bacterial cells, and it extends from the cytoplasmic leaflet of the plasma membrane to the outer layer(s) of wall and capsular polymers. Also, it constitutes an important functional compartment to organize essential metabolic processes, such as solute transport, protein translocation, and respiratory/photorespiratory energy generation. As a mesh-like cell wall heteropolymer that completely surrounds the cell, the peptidoglycan (PG) 4 sacculus confers strength, support, and shape to bacteria (all but the mycoplasmas), as well as resistance to internal turgor pressures (1). Consequently, maintaining the integrity of PG is essential to bacterial viability, which is reflected by the number of different classes of clinically important antibiotics that target its biosynthesis. The list of these include the glycopeptide vancomycin and the ␤-lactams (penicillins, cephalosporins, and monobactams). The PG sacculus is also the target of the antibacterial enzyme lysozyme (EC 3.2.1.17; muramidase), which is present at high concentrations in animal secretions, including tears and saliva, as well as representing a major component of the innate immune system (reviewed in Ref.2).The PG sacculus is not a static structure, but rather it is continually expanded as cells grow. Its metabolism also involves its cleavage for the creation of both pores for secretion systems and sites for the insertion of flagella, in addition to the lysis of septa during cell division (3). A key class of endogenous enzymes responsible for PG lysis are the lytic transglycosylases (LTs) (4). The LTs cleave PG with the same specificity as the lysozyme, that is, the ␤-1,4-glycosidic bond between MurNAc and GlcNAc residues (Fig. 1). However, unlike lysozyme, LTs are not hydrolases as they cleave PG with the concomitant formation of an intramolecular 1,6-anhydromuramoyl reaction product (5).The activit...

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“…Ivy, on the other hand, weakly inhibited g-type lysozyme from goose egg white (GEWL) [19] but not from salmon (SalG). Using homology modeling, protein-protein docking and molecular dynamics simulations, Kyomuhendo et al [20] were able to explain the weak interaction of Ivy with GEWL, and predicted that none of the known fish g-type lysozymes would be inhibited because of their different electrostatic surface properties and curvature. Further, a unique feature of all g-type lysozymes, both from terrestrial and from aquatic organisms, is the involvement of three active residues Glu 73 , Asp 86 en Asp 97 (numbering as in GEWL) [7,[20][21][22].…”

Section: Introductionmentioning

confidence: 99%

“…Using homology modeling, protein-protein docking and molecular dynamics simulations, Kyomuhendo et al [20] were able to explain the weak interaction of Ivy with GEWL, and predicted that none of the known fish g-type lysozymes would be inhibited because of their different electrostatic surface properties and curvature. Further, a unique feature of all g-type lysozymes, both from terrestrial and from aquatic organisms, is the involvement of three active residues Glu 73 , Asp 86 en Asp 97 (numbering as in GEWL) [7,[20][21][22]. While Glu 73 has obvious counterparts in c-and i-type lysozyme (respectively Glu 35 and Glu 11 ) [2,21], the latter have only one aspartate residue (respectively Asp 52 and Asp 30 ) contributing to catalysis.…”

Section: Introductionmentioning

confidence: 99%

Identification of a bacterial inhibitor against g-type lysozyme

Vanderkelen

Herreweghe

Vanoirbeek

et al. 2010

Cell. Mol. Life Sci.

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Lysozymes are antibacterial effectors of the innate immune system in animals that hydrolyze peptidoglycan. Bacteria have evolved protective mechanisms that contribute to lysozyme tolerance such as the production of lysozyme inhibitors, but only inhibitors of chicken (c-) and invertebrate (i-) type lysozyme have been identified. We here report the discovery of a novel Escherichia coli inhibitor specific for goose (g-) type lysozymes, which we designate PliG (periplasmic lysozyme inhibitor of g-type lysozyme). Although it does not inhibit c- or i-type lysozymes, PliG shares a structural sequence motif with the previously described PliI and MliC/PliC lysozyme inhibitor families, suggesting a common ancestry and mode of action. Deletion of pliG increased the sensitivity of E. coli to g-type lysozyme. The existence of inhibitors against all major types of animal lysozyme and their contribution to lysozyme tolerance suggest that lysozyme inhibitors may play a role in bacterial interactions with animal hosts.

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Structural evidence for lack of inhibition of fish goose-type lysozymes by a bacterial inhibitor of lysozyme

Cited by 13 publications

References 43 publications

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

The Vertebrate Lysozyme Inhibitor Ivy Functions to Inhibit the Activity of Lytic Transglycosylase

Identification of a bacterial inhibitor against g-type lysozyme

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