Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Lee, Mi Hee; Osaki, Tsukasa; Lee, Joo Young; Baek, Min Ji; Zhang, Rong; Park, Ji Won; Kawabata, Shun Ichiro; Söderhäll, Kenneth; Lee, Bok Luel

doi:10.1074/jbc.m309821200

Cited by 89 publications

(62 citation statements)

References 52 publications

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“…It may be that PGRPs bind common moieties or secondary structures in their target molecules or, alternatively, that they have binding sites for more than one microbial component. The report that Holotrichia PGRP-S binds laminaripentaose, a component of the fungal cell wall (15), is consistent with the hypothesis that PGRPs recognize diverse microbial ligands by conserved or similar oligosaccharide moieties. Unlike the TLRs, mammalian PGRPs have not been shown to act in signaling, although Drosophila PGRPs are involved in both immune signaling cascades (4,5,9,17,36,37).…”

Section: Discussionsupporting

confidence: 84%

“…Recent studies suggest that microbial recognition by PGRPs may not depend on PGN exclusively. Bovine PGRP-S has been shown to kill microorganisms in which PGN is either buried (Gram-negative bacteria) or absent (Cryptococcus neoformans) (10), and Holotrichia PGRP-S has been shown to trigger an insect immune response by specifically binding 1,3-␤-glucan (15). In addition, soluble murine PGRP-L can mediate macrophage responses to LPS (16).…”

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confidence: 99%

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Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Tydell

Yuan²,

Tran³

et al. 2006

The Journal of Immunology

104

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Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern recognition molecules of innate immunity that are conserved from insects to humans. Various PGRPs are reported to have diverse functions: they bind bacterial molecules, digest PGN, and are essential to the Toll pathway in Drosophila. One family member, bovine PGN recognition protein-S (bPGRP-S), has been found to bind and kill microorganisms in a PGN-independent manner, raising questions about the identity of the bPGRP-S ligand. Addressing this, we have determined the binding and microbicidal properties of bPGRP-S in a range of solutions approximating physiologic conditions. In this study we show that bPGRP-S interacts with other bacterial components, including LPS and lipoteichoic acid, with higher affinities than for PCP, as determined by their abilities to inhibit bPGRP-S-mediated killing of bacteria. Where and how PGRPs act in vivo is not yet clear. Using Immunogold electron microscopy, PGRP-S was localized to the dense/large granules of naive neutrophils, which contain the oxygen-independent bactericidal proteins of these cells, and to the neutrophil phagolysosome. In addition, Immunogold staining and secretion studies demonstrate that neutrophils secrete PGRP-S when exposed to bacteria. Bovine PGRP-S can mediate direct lysis of heat-killed bacteria; however, PGRP-S-mediated killing of bacteria is independent of this activity. Evidence that bPGRP-S has multiple activities and affinity to several bacterial molecules challenges the assumption that the PGRP family of proteins recapitulates the evolution of TLRs. Mammalian PGRPs do not have a single antimicrobial activity against a narrow range of target organisms; rather, they are generalists in their affinity and activity.

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Section: Discussionsupporting

confidence: 84%

mentioning

confidence: 99%

Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Tydell

Yuan²,

Tran³

et al. 2006

The Journal of Immunology

104

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“…A second area of emphasis has been in understanding how infection by microorganisms activates the PO cascade. This has led to the identification of PRRs in B. mori and several other species that activate the PO cascade when they bind microbial cell wall components (33)(34)(35). Studies in this area have also shed important light on the function of SPHs as PAP cofactors (47,48) and as proteins that bind to PO and microbial cell wall components to form complexes that localize melanin deposition to the surface of bacteria (27,28,38,40).…”

Section: Discussionmentioning

confidence: 99%

“…In the case of M. sexta or T. molitor, hemolymph collected from a wound site melanizes weakly or not at all after collection, but the addition of microbial cell wall components alone or together with a diphenolic substrate induces melanization due to binding by pattern recognition receptors like peptidoglycan recognition protein (31,32). Recognition of ␤-1,3-glucan by peptidoglycan recognition protein similarly activates the PO cascade in the beetle H. diomphalia, the crayfish Pacifastacus leniusculus, and B. mori (33)(34)(35). However, early studies of B. mori suggest that, unlike M. sexta and T. molitor, B. mori hemolymph rapidly melanizes without adding a microbial elicitor or diphenol substrate directly to plasma samples (36).…”

Section: B Mori Plasma Rapidly Melanizes After Collection From Amentioning

confidence: 99%

Hemolymph Melanization in the Silkmoth Bombyx mori Involves Formation of a High Molecular Mass Complex That Metabolizes Tyrosine

Clark

Strand

2013

Journal of Biological Chemistry

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Background:The phenoloxidase (PO) cascade regulates the melanization of blood in insects and other arthropods. Results: Hemolymph from Bombyx mori rapidly melanizes after wounding and forms a complex that uses tyrosine as the substrate. Conclusion: Tyrosine usage requires formation of a phenoloxidase-containing complex. Significance: Processing of prophenoloxidase is an intermediate step in the phenoloxidase cascade.

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“…Holotrichia PGRPs recognized both bacterial PGN and fungal ␤-1,3-D-glucan (9), but Tenebrio ␤GRP specifically recognized only fungal 1,3-␤-D-glucan (10). Tenebrio PGRP recognized both the Lys-type and diaminopimelic acid-type PGN (11).…”

mentioning

confidence: 99%

A Novel 40-kDa Protein Containing Six Repeats of an Epidermal Growth Factor-Like Domain Functions as a Pattern Recognition Protein for Lipopolysaccharide

Cho

Brade

et al. 2006

The Journal of Immunology

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Determination of structures and functions of pattern recognition proteins are important for understanding pathogen recognition mechanisms in host defense and for elucidating the activation mechanism of innate immune reactions. In this study, a novel 40-kDa protein, named LPS recognition protein (LRP), was purified to homogeneity from the cell-free plasma of larvae of the large beetle, Holotrichia diomphalia. LRP exhibited agglutinating activities on Escherichia coli, but not on Staphylococcus aureus and Candida albicans. This E. coli-agglutinating activity was preferentially inhibited by the rough-type LPS with a complete core oligosaccharide. LRP consists of 317 aa residues and six repeats of an epidermal growth factor-like domain. Recombinant LRP expressed in a baculovirus system also showed E. coli agglutination activity in vitro and was able to neutralize LPS by inhibition of LPS-induced IL-6 production in mouse bone marrow mast cells. Furthermore, E. coli coated with the purified LRP were more rapidly cleared in the Holotrichia larvae than only E. coli, indicating that this protein participates in the clearance of E. coli in vivo. The three amino-terminal epidermal growth factor-like domains of LRP, but not the three carboxyl epidermal growth factor-like domains, are involved in the LPS-binding activity. Taken together, this LRP functions as a pattern recognition protein for LPS and plays a role as an innate immune protein.

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Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Cited by 89 publications

References 52 publications

Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Hemolymph Melanization in the Silkmoth Bombyx mori Involves Formation of a High Molecular Mass Complex That Metabolizes Tyrosine

A Novel 40-kDa Protein Containing Six Repeats of an Epidermal Growth Factor-Like Domain Functions as a Pattern Recognition Protein for Lipopolysaccharide

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