메뉴 건너뛰기




Volumn 64, Issue 11, 2007, Pages 1395-1402

The peptidoglycan recognition proteins LCa and LCx

Author keywords

Insect innate immunity; Peptidoglycan; PGRP LCa; PGRP LCx

Indexed keywords

MEMBRANE RECEPTOR; PEPTIDOGLYCAN; PEPTIDOGLYCAN RECOGNITION PROTEIN; PEPTIDOGLYCAN RECOGNITION PROTEIN LCA; PEPTIDOGLYCAN RECOGNITION PROTEIN LCX; PROTEIN; UNCLASSIFIED DRUG;

EID: 34250006780     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-6567-3     Document Type: Review
Times cited : (4)

References (39)
  • 1
    • 0029884417 scopus 로고    scopus 로고
    • Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • Yoshida, H., Kinoshita, K. and Ashida, M. (1996). Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J. Biol. Chem. 271, 13854-60.
    • (1996) J. Biol. Chem , vol.271 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3
  • 2
    • 33845586621 scopus 로고    scopus 로고
    • The peptidoglycan recognition proteins (PGRPs)
    • Dziarski, R. and Gupta, D. (2006). The peptidoglycan recognition proteins (PGRPs). Genome Biol. 7, 232.
    • (2006) Genome Biol , vol.7 , pp. 232
    • Dziarski, R.1    Gupta, D.2
  • 3
    • 1642322072 scopus 로고    scopus 로고
    • Drosophila melanogaster innate immunity: An emerging role for peptidoglycan recognition proteins in bacteria detection
    • Royet, J. (2004). Drosophila melanogaster innate immunity: an emerging role for peptidoglycan recognition proteins in bacteria detection. Cell. Mol. Life Sci. 61, 537-46.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 537-546
    • Royet, J.1
  • 4
    • 0034610370 scopus 로고    scopus 로고
    • A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster
    • Werner, T., Liu, G., Kang, D., Ekengren, S., Steiner, H. and Hultmark, D. (2000). A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 97, 13772-7.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13772-13777
    • Werner, T.1    Liu, G.2    Kang, D.3    Ekengren, S.4    Steiner, H.5    Hultmark, D.6
  • 5
    • 0035860732 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: A novel family of four human innate immunity pattern recognition molecules
    • Liu, C., Xu, Z., Gupta, D. and Dziarski, R. (2001). Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J. Biol. Chem. 276, 34686-94.
    • (2001) J. Biol. Chem , vol.276 , pp. 34686-34694
    • Liu, C.1    Xu, Z.2    Gupta, D.3    Dziarski, R.4
  • 6
    • 0033597134 scopus 로고    scopus 로고
    • A pattern recognition protein for peptidoglycan: Cloning the cDNA and the gene of the silkworm, Bombyx mori
    • Ochiai, M. and Ashida, M. (1999). A pattern recognition protein for peptidoglycan: cloning the cDNA and the gene of the silkworm, Bombyx mori. J. Biol. Chem. 274, 11854-8.
    • (1999) J. Biol. Chem , vol.274 , pp. 11854-11858
    • Ochiai, M.1    Ashida, M.2
  • 7
    • 0032544089 scopus 로고    scopus 로고
    • A peptidoglycan recognition protein in innate immunity conserved from insects to humans
    • Kang, D., Liu, G., Lundstrom, A., Gelius, E. and Steiner, H. (1998). A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc. Natl. Acad. Sci. USA 95, 10078-82.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10078-10082
    • Kang, D.1    Liu, G.2    Lundstrom, A.3    Gelius, E.4    Steiner, H.5
  • 8
    • 0023663369 scopus 로고
    • T7 lysozyme inhibits transcription by T7 RNA polymerase
    • Moffatt, B. A. and Studier, F. W. (1987). T7 lysozyme inhibits transcription by T7 RNA polymerase. Cell 49, 221-7.
    • (1987) Cell , vol.49 , pp. 221-227
    • Moffatt, B.A.1    Studier, F.W.2
  • 9
    • 0037470091 scopus 로고    scopus 로고
    • A scavenger function for a Drosophila peptidoglycan recognition protein
    • Mellroth, P., Karlsson, J. and Steiner, H. (2003). A scavenger function for a Drosophila peptidoglycan recognition protein. J. Biol. Chem. 278, 7059-64.
    • (2003) J. Biol. Chem , vol.278 , pp. 7059-7064
    • Mellroth, P.1    Karlsson, J.2    Steiner, H.3
  • 11
    • 33645236166 scopus 로고    scopus 로고
    • Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor
    • Chang, C. I., Chelliah, Y., Borek, D., Mengin-Lecreulx, D. and Deisenhofer, J. (2006). Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science 311, 1761-4.
    • (2006) Science , vol.311 , pp. 1761-1764
    • Chang, C.I.1    Chelliah, Y.2    Borek, D.3    Mengin-Lecreulx, D.4    Deisenhofer, J.5
  • 12
    • 22544477068 scopus 로고    scopus 로고
    • Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition
    • Chang, C. I., Ihara, K., Chelliah, Y., Mengin-Lecreulx, D., Wakatsuki, S. and Deisenhofer, J. (2005). Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition. Proc. Natl. Acad. Sci. USA 102, 10279-84.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10279-10284
    • Chang, C.I.1    Ihara, K.2    Chelliah, Y.3    Mengin-Lecreulx, D.4    Wakatsuki, S.5    Deisenhofer, J.6
  • 15
    • 0035856990 scopus 로고    scopus 로고
    • Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein
    • Michel, T., Reichhart, J. M., Hoffmann, J. A. and Royet, J. (2001). Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 414, 756-9.
    • (2001) Nature , vol.414 , pp. 756-759
    • Michel, T.1    Reichhart, J.M.2    Hoffmann, J.A.3    Royet, J.4
  • 16
    • 9244251126 scopus 로고    scopus 로고
    • Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria
    • Bischoff, V., Vignal, C., Boneca, I. G., Michel, T., Hoffmann, J. A. and Royet, J. (2004). Function of the Drosophila pattern-recognition receptor PGRP-SD in the detection of Gram-positive bacteria. Nat. Immunol. 5, 1175-80.
    • (2004) Nat. Immunol , vol.5 , pp. 1175-1180
    • Bischoff, V.1    Vignal, C.2    Boneca, I.G.3    Michel, T.4    Hoffmann, J.A.5    Royet, J.6
  • 18
    • 10644267665 scopus 로고    scopus 로고
    • Peptidoglycan recognition protein (PGRP)-LE and PGRP-LC act synergistically in Drosophila immunity
    • Takehana, A., Yano, T., Mita, S., Kotani, A., Oshima, Y. and Kurata, S. (2004). Peptidoglycan recognition protein (PGRP)-LE and PGRP-LC act synergistically in Drosophila immunity. EMBO J. 23, 4690-700.
    • (2004) EMBO J , vol.23 , pp. 4690-4700
    • Takehana, A.1    Yano, T.2    Mita, S.3    Kotani, A.4    Oshima, Y.5    Kurata, S.6
  • 19
    • 33645770760 scopus 로고    scopus 로고
    • Bischoff, V., Vignal, C., Duvic, B., Boneca, I. G., Hoffmann, J. A. and Royet, J. (2006). Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2. PLoS Pathog. 2, e14.
    • Bischoff, V., Vignal, C., Duvic, B., Boneca, I. G., Hoffmann, J. A. and Royet, J. (2006). Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2. PLoS Pathog. 2, e14.
  • 21
    • 19044388766 scopus 로고    scopus 로고
    • Structure and metabolism of peptidoglycan and molecular requirements allowing its detection by the Drosophila innate immune system
    • Mengin-Lecreulx, D. and Lemaitre, B. (2005). Structure and metabolism of peptidoglycan and molecular requirements allowing its detection by the Drosophila innate immune system. J. Endotoxin Res. 11, 105-11.
    • (2005) J. Endotoxin Res , vol.11 , pp. 105-111
    • Mengin-Lecreulx, D.1    Lemaitre, B.2
  • 22
    • 0020071653 scopus 로고
    • Detection, isolation, and analysis of a released Bordetella pertussis product toxic to cultured tracheal cells
    • Goldman, W. E., Klapper, D. G. and Baseman, J. B. (1982). Detection, isolation, and analysis of a released Bordetella pertussis product toxic to cultured tracheal cells. Infect. Immun. 36, 782-94.
    • (1982) Infect. Immun , vol.36 , pp. 782-794
    • Goldman, W.E.1    Klapper, D.G.2    Baseman, J.B.3
  • 23
    • 12844279852 scopus 로고    scopus 로고
    • Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor
    • Choe, K. M., Lee, H. and Anderson, K. V. (2005). Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor. Proc. Natl. Acad. Sci. USA 102, 1122-6.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1122-1126
    • Choe, K.M.1    Lee, H.2    Anderson, K.V.3
  • 24
    • 0037066464 scopus 로고    scopus 로고
    • Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila
    • Choe, K. M., Werner, T., Stoven, S., Hultmark, D. and Anderson, K. V. (2002). Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila. Science 296, 359-62.
    • (2002) Science , vol.296 , pp. 359-362
    • Choe, K.M.1    Werner, T.2    Stoven, S.3    Hultmark, D.4    Anderson, K.V.5
  • 25
    • 0037061450 scopus 로고    scopus 로고
    • The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein
    • Gottar, M., Gobert, V., Michel, T., Belvin, M., Duyk, G., Hoffmann, J. A., Ferrandon, D. and Royet, J. (2002). The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 416, 640-4.
    • (2002) Nature , vol.416 , pp. 640-644
    • Gottar, M.1    Gobert, V.2    Michel, T.3    Belvin, M.4    Duyk, G.5    Hoffmann, J.A.6    Ferrandon, D.7    Royet, J.8
  • 26
    • 0037061482 scopus 로고    scopus 로고
    • Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli
    • Ramet, M., Manfruelli, P., Pearson, A., Mathey-Prevot, B. and Ezekowitz, R. A. (2002). Functional genomic analysis of phagocytosis and identification of a Drosophila receptor for E. coli. Nature 416, 644-8.
    • (2002) Nature , vol.416 , pp. 644-648
    • Ramet, M.1    Manfruelli, P.2    Pearson, A.3    Mathey-Prevot, B.4    Ezekowitz, R.A.5
  • 28
    • 0033231556 scopus 로고    scopus 로고
    • Relish, a central factor in the control of humoral but not cellular immunity in Drosophila
    • Hedengren, M., Asling, B., Dushay, M. S., Ando, I., Ekengren, S., Wihlborg, M. and Hultmark, D. (1999). Relish, a central factor in the control of humoral but not cellular immunity in Drosophila. Mol. Cell 4, 827-37.
    • (1999) Mol. Cell , vol.4 , pp. 827-837
    • Hedengren, M.1    Asling, B.2    Dushay, M.S.3    Ando, I.4    Ekengren, S.5    Wihlborg, M.6    Hultmark, D.7
  • 30
    • 3843067734 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha
    • Guan, R., Malchiodi, E. L., Wang, Q., Schuck, P. and Mariuzza, R. A. (2004). Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha. J. Biol. Chem. 279, 31873-82.
    • (2004) J. Biol. Chem , vol.279 , pp. 31873-31882
    • Guan, R.1    Malchiodi, E.L.2    Wang, Q.3    Schuck, P.4    Mariuzza, R.A.5
  • 31
    • 0042195829 scopus 로고    scopus 로고
    • Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster
    • Kim, M. S., Byun, M. and Oh, B. H. (2003). Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat. Immunol. 4, 787-93.
    • (2003) Nat. Immunol , vol.4 , pp. 787-793
    • Kim, M.S.1    Byun, M.2    Oh, B.H.3
  • 32
    • 3042613815 scopus 로고    scopus 로고
    • Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution
    • Reiser, J. B., Teyton, L. and Wilson, I. A. (2004). Crystal structure of the Drosophila peptidoglycan recognition protein (PGRP)-SA at 1.56 A resolution. J. Mol. Biol. 340, 909-17.
    • (2004) J. Mol. Biol , vol.340 , pp. 909-917
    • Reiser, J.B.1    Teyton, L.2    Wilson, I.A.3
  • 34
    • 0032527832 scopus 로고    scopus 로고
    • Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme
    • Jeruzalmi, D. and Steitz, T. A. (1998). Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme. EMBO J. 17, 4101-13.
    • (1998) EMBO J , vol.17 , pp. 4101-4113
    • Jeruzalmi, D.1    Steitz, T.A.2
  • 36
    • 33750091050 scopus 로고    scopus 로고
    • PGRP-SB1: An N-acetylmuramoyl L-alanine amidase with antibacterial activity
    • Mellroth, P. and Steiner, H. (2006). PGRP-SB1: an N-acetylmuramoyl L-alanine amidase with antibacterial activity. Biochem. Biophys. Res. Commun. 350, 994-9.
    • (2006) Biochem. Biophys. Res. Commun , vol.350 , pp. 994-999
    • Mellroth, P.1    Steiner, H.2
  • 37
    • 33646378677 scopus 로고    scopus 로고
    • Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins
    • Lim, J. H., Kim, M. S., Kim, H. E., Yano, T., Oshima, Y., Aggarwal, K., Goldman, W. E., Silverman, N., Kurata, S. and Oh, B. H. (2006). Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins. J. Biol. Chem. 281, 8286-95.
    • (2006) J. Biol. Chem , vol.281 , pp. 8286-8295
    • Lim, J.H.1    Kim, M.S.2    Kim, H.E.3    Yano, T.4    Oshima, Y.5    Aggarwal, K.6    Goldman, W.E.7    Silverman, N.8    Kurata, S.9    Oh, B.H.10
  • 39
    • 0037020201 scopus 로고    scopus 로고
    • Christophides, G. K., Zdobnov, E., Barillas-Mury, C., Birney, E., Blandin, S., Blass, C., Brey, P. T., Collins, F. H., Danielli, A., Dimopoulos, G., Hetru, C., Hoa, N. T., Hoffmann, J. A., Kanzok, S. M., Letunic, I., Levashina, E. A., Loukeris, T. G., Lycett, G., Meister, S., Michel, K., Moita, L. F., Muller, H. M., Osta, M. A., Paskewitz, S. M., Reichhart, J. M., Rzhetsky, A., Troxler, L., Vernick, K. D., Vlachou, D., Volz, J., von Mering, C., Xu, J., Zheng, L., Bork, P. and Kafatos, F. C. (2002). Immunity-related genes and gene families in Anopheles gambiae. Science 298, 159-65.
    • Christophides, G. K., Zdobnov, E., Barillas-Mury, C., Birney, E., Blandin, S., Blass, C., Brey, P. T., Collins, F. H., Danielli, A., Dimopoulos, G., Hetru, C., Hoa, N. T., Hoffmann, J. A., Kanzok, S. M., Letunic, I., Levashina, E. A., Loukeris, T. G., Lycett, G., Meister, S., Michel, K., Moita, L. F., Muller, H. M., Osta, M. A., Paskewitz, S. M., Reichhart, J. M., Rzhetsky, A., Troxler, L., Vernick, K. D., Vlachou, D., Volz, J., von Mering, C., Xu, J., Zheng, L., Bork, P. and Kafatos, F. C. (2002). Immunity-related genes and gene families in Anopheles gambiae. Science 298, 159-65.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.