참고문헌
- Berry, A.M., Lock, R.A., Hansman, D., and Paton, J.C. (1989). Contribution of autolysin to virulence of Streptococcus pneumoniae. Infect. Immun. 57, 2324-2330.
- Canvin, J.R., Marvin, A.P., Sivakumaran, M., Paton, J.C., Boulnois, G.J., Andrew, P.W., and Mitchell, T.J. (1995). The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus. J. Infect. Dis. 172, 119-123. https://doi.org/10.1093/infdis/172.1.119
- Chakravortty, D., Koide, N., Kato, Y., Sugiyama, T., Mu, M.M., Yoshida, T., and Yokochi, T. (2000). The inhibitory action of butyrate on lipopolysaccharide-induced nitric oxide production in RAW 264.7 murine macrophage cells. J. Endotoxin. Res. 6, 243-247. https://doi.org/10.1177/09680519000060030501
- Gacser, A., Trofa, D., Schafer, W., and Nosanchuk, J.D. (2007). Targeted gene deletion in Candida parapsilosis demonstrates the role of secreted lipase in virulence. J. Clin Invest. 117, 3049-3058. https://doi.org/10.1172/JCI32294
- Gill, S.R., Fouts, D.E., Archer, G.L., Mongodin, E.F., DeBoy, R.T., Ravel, J., Paulsen, I.T., Kolonay, J.F., Brinkac, L., Beanan, M., et al. (2005). Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain. J. Bacteriol. 187, 2426-2438. https://doi.org/10.1128/JB.187.7.2426-2438.2005
- Hajaj, B., Yesilkaya, H., Benisty, R., David, M., Andrew, P.W., and Porat, N. (2012). Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments. Infect. Immun. 80, 4333-4343. https://doi.org/10.1128/IAI.00126-12
- Hirst, R.A., Gosai, B., Rutman, A., Guerin, C.J., Nicotera, P., Andrew, P.W., and O'Callaghan, C. (2008). Streptococcus pneumoniae deficient in pneumolysin or autolysin has reduced virulence in meningitis. J. Infect Dis. 197, 744-751. https://doi.org/10.1086/527322
- Jorgensen, S., Skov, K.W., and Diderichsen, B. (1991). Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes. J. Bacteriol. 173, 559-567. https://doi.org/10.1128/jb.173.2.559-567.1991
- Jaeger, K.-E., Ransac, S., Dijkstra, B.W., Colson, C., van Heuvel, M., and Misset, O. (1994). Bacterial lipases. FEMS Microbiol. Rev. 15, 29-63. https://doi.org/10.1111/j.1574-6976.1994.tb00121.x
- Joseph, B., Ramteke, P.W., and Thomas, G. (2008). Cold active microbial lipases: some hot issues and recent developments. Biotechnol. Adv. 26, 457-470. https://doi.org/10.1016/j.biotechadv.2008.05.003
- Kadioglu, A., Weiser, J.N., Paton, J.C., and Andrew, P.W. (2008). The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease. Nat. Rev. Micro. 6, 288-301. https://doi.org/10.1038/nrmicro1871
- Kang, N.-S., Park, S.-Y., Lee, K.-R., Lee, S.-M., Lee, B.-G., Shin, D.-H., and Pyo, S. (2002). Modulation of macrophage function activity by ethanolic extract of larvae of Holotrichia diomphalia. J. Ethnopharmacol. 79, 89-94. https://doi.org/10.1016/S0378-8741(01)00369-5
- Kerttula, Y., and Weber, T. (1987). Serum lipids in pneumonia of different aetiology. Ann. Clin. Res. 20, 184-188.
- Kwon, H.-Y., Kim, S.-W., Choi, M.-H., Ogunniyi, A.D., Paton, J.C., Park, S.-H., Pyo, S.-N., and Rhee, D.-K. (2003). Effect of heat shock and mutations in ClpL and ClpP on virulence gene expression in Streptococcus pneumoniae. Infect. Immun. 71, 3757-3765. https://doi.org/10.1128/IAI.71.7.3757-3765.2003
- Lanie, J.A., Ng, W.-L., Kazmierczak, K.M., Andrzejewski, T.M., Davidsen, T.M., Wayne, K.J., Tettelin, H., Glass, J.I., and Winkler, M.E. (2007). Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6. J. Bacteriol. 189, 38-51. https://doi.org/10.1128/JB.01148-06
- Liu, L., Johnson, H.L., Cousens, S., Perin, J., Scott, S., Lawn, J.E., Rudan, I., Campbell, H., Cibulskis, R., and Li, M. (2012). Global, regional, and national causes of child mortality: an updated systematic analysis for 2010 with time trends since 2000. The Lancet 379, 2151-2161. https://doi.org/10.1016/S0140-6736(12)60560-1
- Lopez, R., and Garcia, E. (2004). Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage. FEMS Microbiol. Rev. 28, 553-580. https://doi.org/10.1016/j.femsre.2004.05.002
- Luong, T.T., Kim, E.-H., Bak, J.P., Nguyen, C.T., Choi, S., Briles, D.E., Pyo, S., and Rhee, D.-K. (2015). Ethanol-induced alcohol dehydrogenase E (AdhE). potentiates pneumolysin in Streptococcus pneumoniae. Infect. Immun. 83, 108-119. https://doi.org/10.1128/IAI.02434-14
- Martin, G.S. (2012). Sepsis, severe sepsis and septic shock: changes in incidence, pathogens and outcomes. Expert Rev. Anti Infect. Ther. 10, 701-706. https://doi.org/10.1586/eri.12.50
- Maslowski, K.M., Vieira, A.T., Ng, A., Kranich, J., Sierro, F., Di, Y., Schilter, H.C., Rolph, M.S., Mackay, F., Artis, D., et al. (2009). Regulation of inflammatory responses by gut microbiota and chemoattractant receptor GPR43. Nature 461, 1282-1286. https://doi.org/10.1038/nature08530
- Mellroth, P., Daniels, R., Eberhardt, A., Ronnlund, D., Blom, H., Widengren, J., Normark, S., and Henriques-Normark, B. (2012). LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan. J. Biol. Chem. 287, 11018-11029. https://doi.org/10.1074/jbc.M111.318584
- Munford, R., and Suffredini, A. (2009). Sepsis, severe sepsis, and septic shock; in Principles and practice of infectious diseases. 7th ed. (Philadelphia: Churchill Livingstone).
- Nawabi, P., Catron, D.M., and Haldar, K. (2008). Esterification of cholesterol by a type III secretion effector during intracellular Salmonella infection. Mol. Microbiol .68, 173-185. https://doi.org/10.1111/j.1365-2958.2008.06142.x
- Nguyen, C.T., Kim, E.-H., Luong, T.T., Pyo, S., and Rhee, D.-K. (2014). ATF3 confers resistance to pneumococcal infection through positive regulation of cytokine production. J. Infect. Dis. 210, 1745-1754. https://doi.org/10.1093/infdis/jiu352
- Orihuela, C.J., Gao, G., Francis, K.P., Yu, J., and Tuomanen, E.I. (2004). Tissue-specific contributions of pneumococcal virulence factors to pathogenesis. J. Infect. Dis. 190, 1661-1669. https://doi.org/10.1086/424596
-
Park, J.-S., Lee, E.-J., Lee, J.-C., Kim, W.-K., and Kim, H.-S. (2007). Anti-inflammatory effects of short chain fatty acids in IFN-
${\gamma}$ -stimulated RAW 264.7 murine macrophage cells: Involvement of NF-${\kappa}B$ and ERK signaling pathways. Int. Immunopharmacol. 7, 70-77. https://doi.org/10.1016/j.intimp.2006.08.015 - Pemberton, J.M., Kidd, S.P., and Schmidt, R. (1997). Secreted enzymes of Aeromonas. FEMS Microbiol. Lett. 152, 1-10. https://doi.org/10.1111/j.1574-6968.1997.tb10401.x
- Pinsirodom, P., and Parkin, K.L. (2001). Lipase Assays; in Current protocols in food analytical chemistry. Unit C3.1.1-C3.1.13 (John Wiley & Sons, Inc.).
- Rollof, J., and Normark, S. (1992). In vivo processing of Staphylococcus aureus lipase. J. Bacteriol. 174, 1844-1847. https://doi.org/10.1128/jb.174.6.1844-1847.1992
- Rollof, J., HedstrOM, S.A., and Nilsson-Ehle, P. (1987). Lipolytic activity of Staphylococcus aureus strains from disseminated and localized infections. APMIS 95B, 109-113.
- Rollof, J., Braconier, J.H., Soderstrom, C., and Nilsson-Ehle, P. (1988). Interference of Staphylococcus aureus lipase with human granulocyte function. Eur. J. Clin. Microbiol. Infect Dis. 7, 505-510. https://doi.org/10.1007/BF01962601
-
Stehr, F., Felk, A., Gacser, A., Kretschmar, M., Mahn
$\ss$ , B., Neuber, K., Hube, B., and Schafer, W. (2004). Expression analysis of the Candida albicans lipase gene family during experimental infections and in patient samples1. FEMS Yeast Res. 4, 401-408. https://doi.org/10.1016/S1567-1356(03)00205-8 - Stratton, C.W., Evans, M.E., Burch, D.J., Hawley, H.B., Horsman, T.A., Tu, K.K., and Reller, L.B. (1986). Effect of human serum on inhibition of growth of Staphylococcus aureus by antimicrobial agents. Eur. J. Clin. Microbiol. 5, 351-353. https://doi.org/10.1007/BF02017797
- Tran, T.D.-H., Kwon, H.-Y., Kim, E.-H., Kim, K.-W., Briles, D.E., Pyo, S., and Rhee, D.-K. (2011). Decrease in penicillin susceptibility due to heat shock protein ClpL in Streptococcus pneumoniae. Antimicrob. Agents Chemother. 55, 2714-2728. https://doi.org/10.1128/AAC.01383-10
- Vinolo, M., Rodrigues, H., Hatanaka, E., Hebeda, C., Farsky, S., and Curi, R. (2009). Short-chain fatty acids stimulate the migration of neutrophils to inflammatory sites. Clin. Sci. (Lond). 117, 331-338. https://doi.org/10.1042/CS20080642
- Voigt, C., von Scheidt, B., Gacser, A., Kassner, H., Lieberei, R., Schafer, W., and Salomon, S. (2007). Enhanced mycotoxin production of a lipase-deficient Fusarium graminearum mutant correlates to toxinrelated gene expression. Eur. J. Plant Pathol. 117, 1-12. https://doi.org/10.1007/s10658-006-9063-y
- Waldecker, M., Kautenburger, T., Daumann, H., Busch, C., and Schrenk, D. (2008). Inhibition of histone-deacetylase activity by shortchain fatty acids and some polyphenol metabolites formed in the colon. J. Nutr. Biochem. 19, 587-593. https://doi.org/10.1016/j.jnutbio.2007.08.002
- Yang, G., Hernandez-Rodriguez, C.S., Beeton, M.L., Wilkinson, P., and Waterfield, N.R. (2012). Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion. PLoS Pathog. 8, e1002692. https://doi.org/10.1371/journal.ppat.1002692
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