乳酸乳球菌噬菌体与宿主相互作用研究进展
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摘要
发酵乳制品主要依靠乳酸菌对牛奶酸化并形成独特的风味。然而,乳酸菌因易受噬菌体感染而导致乳制品发酵缓慢甚至失败,这对乳制品行业造成巨大的经济损失。乳酸乳球菌是发酵乳制品行业中应用十分广泛的一种乳酸菌,目前其宿主上的受体分子和相应噬菌体受体结合蛋白结构分析方面的研究已经取得一定进展。这些乳酸乳球菌模型系统对加深其他乳酸菌噬菌体-宿主相互作用的认识、揭示不同乳酸菌噬菌体-宿主相互作用机制的异同提供理论依据。本文综述了目前所发现的乳酸乳球菌噬菌体及其宿主之间的相互作用,探讨受体主要成分与编码受体结合蛋白基因的研究,为研究其他乳酸菌噬菌体种群及防治措施提供一定的理论基础。
Fermented dairy products rely primarily on lactic acid bacteria to acidify milk and form unique flavors. However,the susceptibility of lactic acid bacteria to phage infection results in slow or even failure of dairy fermentation,which causes huge economic losses to the dairy industry. Lactococcus lactis is a lactic acid bacteria widely used in the fermented dairy industry. At present,research on the structural analysis of receptor molecules of the Lactococcus lactis host and the corresponding phage-encoded receptor-binding proteins has made some progress. These Lactococcus lactis model systems are expanding toward understanding phage-host interactions of other lactic acid bacteria and revealing the similarities and differences between these interactions. In this paper,the interactions between the currently discovered Lactococcus lactis phage and their hosts,and explored the research progress of the main components of receptors and the genes encoding receptor-binding proteins are reviewed,which provides a theoretical basis for studying the phage populations and control measures of other lactic acid bacteria.
Fermented dairy products rely primarily on lactic acid bacteria to acidify milk and form unique flavors. However,the susceptibility of lactic acid bacteria to phage infection results in slow or even failure of dairy fermentation,which causes huge economic losses to the dairy industry. Lactococcus lactis is a lactic acid bacteria widely used in the fermented dairy industry. At present,research on the structural analysis of receptor molecules of the Lactococcus lactis host and the corresponding phage-encoded receptor-binding proteins has made some progress. These Lactococcus lactis model systems are expanding toward understanding phage-host interactions of other lactic acid bacteria and revealing the similarities and differences between these interactions. In this paper,the interactions between the currently discovered Lactococcus lactis phage and their hosts,and explored the research progress of the main components of receptors and the genes encoding receptor-binding proteins are reviewed,which provides a theoretical basis for studying the phage populations and control measures of other lactic acid bacteria.
引文
[1]王丽丽.乳酸菌生物技术的发展[J].现代食品,2016(20):31-32.
[2]李海涛,王慕华,赵玉明,等.酸奶生产中噬菌体污染的判断及防治[J].中国乳品工业,2018(3):13-15.
[3]Wagner N,Samtlebe M,Franz C M A P,et al.Dairy bacteriophages isolated from whey powder:Thermal inactivation and kinetic characterisation[J].International Dairy Journal,2017,68:95-104.
[4]Mahony J,Oliveira J,Collins B,et al.Genetic and functional characterisation of the lactococcal P335 phage-host interactions[J].BMC Genomics,2017,18(1):146.
[5]Spinelli S,Veesler D,Bebeacua C,et al.Structures and host-adhesion mechanisms of lactococcal siphophages[J].Frontiers in Microbiology,2014,5:3.
[6]Mahony J,Ainsworth S,Stockdale S,et al.Phages of lactic acid bacteria:The role of genetics in understanding phage-host interactions and their co-evolutionary processes[J].Virology,2012,434(2):143-150.
[7]Mahony J,Bottacini F,Van sinderen D,et al.Progress in lactic acid bacterial phage research[J].Microbial Cell Factories,2014,13(1):S1.
[8]于美玲.两株乳杆菌噬菌体的分离鉴定及抗噬菌体菌株的筛选[D].哈尔滨:东北农业大学,2015.
[9]Brüssow H,Hendrix R W.Phage genomics:Small is beautiful[J].Cell,2002,108(1):13-16.
[10]张勇.益生菌乳制品货架期质量分析与研究[D].西安:陕西科技大学,2018.
[11]Mahony J,Cambillau C,Van sinderen D.Host recognition by lactic acid bacterial phages[J].FEMS Microbiology Reviews,2017,41(1):S16-S26.
[12]Deveau H,Labrie S J,Chopin M C,et al.Biodiversity and classification of lactococcal phages[J].Applied and Environmental Microbiology,2006,72(6):4338-4346.
[13]习羽,汪政煜,张和平,等.乳酸菌抗噬菌体相关机理的研究进展[J].乳业科学与技术,2015,38(6):22-26.
[14]Forde A,Fitzgerald G F.Bacteriophage defence systems in lactic acid bacteria[J].Antonie Van Leeuwenhoek,1999,76(1-4):89-113.
[15]Heller K,Braun V.Polymannose o-antigens of Escherichia coli,the binding-sites for the reversible adsorption of bacteriophage-T5+ via the L-shaped tail fibers[J].Journal of Virology,1982,41(1):222-227.
[16]Dupont K,Janzen T,Vogensen F K,et al.Identification of Lactococcus lactis genes required for bacteriophage adsorption[J].Applied and Environmental Microbiology,2004,70(10):5825-5832.
[17]Geller B L,Ivey R G,Trempy J E,et al.Cloning of a chromosomal gene required for phage infection of Lactococcus lactis subsp.lactis C2[J].Journal of Bacteriology,1993,175(17):5510-5519.
[18]Dupont K,Vogensen F K,Neve H,et al.Identification of the receptor-binding protein in 936-species lactococcal bacteriophages[J].Applied and Environmental Microbiology,2004,70(10):5818-5824.
[19]Vegge C S,Vogensen F K,Mc grath S,et al.Identification of the lower baseplate protein as the antireceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009[J].Journal of Bacteriology,2006,188(1):55-63.
[20]Mahony J,Kot W,Murphy J,et al.Investigation of the relationship between lactococcal host cell wall polysaccharide genotype and 936 phage receptor binding protein phylogeny[J].Applied and Environmental Microbiology,2013,79(14):4385-4392.
[21]Spinelli S,Campanacci V,Blangy S,et al.Modular structure of the receptor binding proteins of Lactococcus lactis phages.The RBP structure of the temperate phage TP901-1[J].The Journal of Biological Chemistry,2006,281(20):14256-14262.
[22]Bebeacua C,Bron P,Lai L,et al.Structure and molecular assignment of lactococcal phage TP901-1 baseplate[J].The Journal of Biological Chemistry,2010,285(50):39079-39086.
[23]Collins B,Bebeacua C,Mahony J,et al.Structure and functional analysis of the host recognition device of lactococcal phage Tuc2009[J].Journal of Virology,2013,87(15):8429-8440.
[24]Sciara G,Bebeacua C,Bron P,et al.Structure of lactococcal phage p2 baseplate and its mechanism of activation[J].Proceedings of the National Academy of Sciences of the United States of America,2010,107(15):6852-6857.
[25]Veesler D,Spinelli S,Mahony J,et al.Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism[J].Proceedings of the National Academy of Sciences of the United States of America,2012,109(23):8954-8958.
[26]Spinelli S,Desmyter A,Verrips C T,et al.Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses[J].Nature Structural & Molecular Biology,2006,13(1):85-89.
[27]Schouler C,Ehrlich S D,Chopin M C.Sequence and organization of the lactococcal prolate-headed bIL67 phage genome[J].Microbiology,1994,140(11):3061-3069.
[28]Monteville M R,Ardestani B,Geller B L.Lactococcal bacteriophages require a host cell wall carbohydrate and a plasma membrane protein for adsorption and ejection of DNA[J].Applied and Environmental Microbiology,1994,60(9):3204-3211.
[29]Mooney D T,Jann M,Geller B L.Subcellular location of phage infection protein(Pip)in Lactococcus lactis[J].Canadian Journal of Microbiology,2006,52(7):664-672.
[30]Mahony J,Van sinderen D.Structural aspects of the interaction of dairy phages with their host bacteria[J].Viruses,2012,4(9):1410-1424.
[31]Munsch-alatossava P,Alatossava T.The extracellular phage-host interactions involved in the bacteriophage LL-H infection of Lactobacillus delbrueckii ssp.lactis ATCC 15808[J].Frontiers in Microbiology,2013,4:408.
[32]Vinogradov E,Sadovskaya I,Grard T,et al.Structural studies of the cell wall polysaccharide from Lactococcus lactis UC509.9[J].Carbohydrate Research,2018,461:25-31.
[33]Sadovskaya I,Vinogradov E,Courtin P,et al.Another brick in the wall:A rhamnan polysaccharide trapped inside peptidoglycan of Lactococcus lactis[J].MBIO,2017,8(5):e01303-e01317.
[34]Ainsworth S,Sadovskaya I,Vinogradov E,et al.Differences in lactococcal cell wall polysaccharide structure are major determining factors in bacteriophage sensitivity[J].MBIO,2014,5(3):e00814-e00880.
[35]Chapot-chartier M P,Vinogradov E,Sadovskaya I,et al.Cell surface of Lactococcus lactis is covered by a protective polysaccharide pellicle[J].The Journal of Biological Chemistry,2010,285(14):10464-10471.
[36]Farenc C,Spinelli S,Vinogradov E,et al.Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by thephage 1358 receptor binding protein[J].Journal of Virology,2014,88(12):7005-7015.
[37]Mccabe O,Spinelli S,Farenc C,et al.The targeted recognition of Lactococcus lactis phages to their polysaccharide receptors[J].Molecular Microbiology,2015,96(4):875-886.
[38]Mahony J,Randazzo W,Neve H,et al.Lactococcal 949 group phages recognize a carbohydrate receptor on the host cell surface[J].Applied and Environmental Microbiology,2015,81(10):3299-3305.
[39]Oliveira J,Mahony J,Hanemaaijer L,et al.Biodiversity of bacteriophages infecting Lactococcus lactis starter cultures[J].Journal of Dairy Science,2018,101(1):96-105.
[40]Legrand P,Collins B,Blangy S,et al.The atomic structure of the phage tuc2009 baseplate tripod suggests that host recognition involves two different carbohydrate binding modules[J].MBIO,2016,7(1):e01715-e01781.
[2]李海涛,王慕华,赵玉明,等.酸奶生产中噬菌体污染的判断及防治[J].中国乳品工业,2018(3):13-15.
[3]Wagner N,Samtlebe M,Franz C M A P,et al.Dairy bacteriophages isolated from whey powder:Thermal inactivation and kinetic characterisation[J].International Dairy Journal,2017,68:95-104.
[4]Mahony J,Oliveira J,Collins B,et al.Genetic and functional characterisation of the lactococcal P335 phage-host interactions[J].BMC Genomics,2017,18(1):146.
[5]Spinelli S,Veesler D,Bebeacua C,et al.Structures and host-adhesion mechanisms of lactococcal siphophages[J].Frontiers in Microbiology,2014,5:3.
[6]Mahony J,Ainsworth S,Stockdale S,et al.Phages of lactic acid bacteria:The role of genetics in understanding phage-host interactions and their co-evolutionary processes[J].Virology,2012,434(2):143-150.
[7]Mahony J,Bottacini F,Van sinderen D,et al.Progress in lactic acid bacterial phage research[J].Microbial Cell Factories,2014,13(1):S1.
[8]于美玲.两株乳杆菌噬菌体的分离鉴定及抗噬菌体菌株的筛选[D].哈尔滨:东北农业大学,2015.
[9]Brüssow H,Hendrix R W.Phage genomics:Small is beautiful[J].Cell,2002,108(1):13-16.
[10]张勇.益生菌乳制品货架期质量分析与研究[D].西安:陕西科技大学,2018.
[11]Mahony J,Cambillau C,Van sinderen D.Host recognition by lactic acid bacterial phages[J].FEMS Microbiology Reviews,2017,41(1):S16-S26.
[12]Deveau H,Labrie S J,Chopin M C,et al.Biodiversity and classification of lactococcal phages[J].Applied and Environmental Microbiology,2006,72(6):4338-4346.
[13]习羽,汪政煜,张和平,等.乳酸菌抗噬菌体相关机理的研究进展[J].乳业科学与技术,2015,38(6):22-26.
[14]Forde A,Fitzgerald G F.Bacteriophage defence systems in lactic acid bacteria[J].Antonie Van Leeuwenhoek,1999,76(1-4):89-113.
[15]Heller K,Braun V.Polymannose o-antigens of Escherichia coli,the binding-sites for the reversible adsorption of bacteriophage-T5+ via the L-shaped tail fibers[J].Journal of Virology,1982,41(1):222-227.
[16]Dupont K,Janzen T,Vogensen F K,et al.Identification of Lactococcus lactis genes required for bacteriophage adsorption[J].Applied and Environmental Microbiology,2004,70(10):5825-5832.
[17]Geller B L,Ivey R G,Trempy J E,et al.Cloning of a chromosomal gene required for phage infection of Lactococcus lactis subsp.lactis C2[J].Journal of Bacteriology,1993,175(17):5510-5519.
[18]Dupont K,Vogensen F K,Neve H,et al.Identification of the receptor-binding protein in 936-species lactococcal bacteriophages[J].Applied and Environmental Microbiology,2004,70(10):5818-5824.
[19]Vegge C S,Vogensen F K,Mc grath S,et al.Identification of the lower baseplate protein as the antireceptor of the temperate lactococcal bacteriophages TP901-1 and Tuc2009[J].Journal of Bacteriology,2006,188(1):55-63.
[20]Mahony J,Kot W,Murphy J,et al.Investigation of the relationship between lactococcal host cell wall polysaccharide genotype and 936 phage receptor binding protein phylogeny[J].Applied and Environmental Microbiology,2013,79(14):4385-4392.
[21]Spinelli S,Campanacci V,Blangy S,et al.Modular structure of the receptor binding proteins of Lactococcus lactis phages.The RBP structure of the temperate phage TP901-1[J].The Journal of Biological Chemistry,2006,281(20):14256-14262.
[22]Bebeacua C,Bron P,Lai L,et al.Structure and molecular assignment of lactococcal phage TP901-1 baseplate[J].The Journal of Biological Chemistry,2010,285(50):39079-39086.
[23]Collins B,Bebeacua C,Mahony J,et al.Structure and functional analysis of the host recognition device of lactococcal phage Tuc2009[J].Journal of Virology,2013,87(15):8429-8440.
[24]Sciara G,Bebeacua C,Bron P,et al.Structure of lactococcal phage p2 baseplate and its mechanism of activation[J].Proceedings of the National Academy of Sciences of the United States of America,2010,107(15):6852-6857.
[25]Veesler D,Spinelli S,Mahony J,et al.Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism[J].Proceedings of the National Academy of Sciences of the United States of America,2012,109(23):8954-8958.
[26]Spinelli S,Desmyter A,Verrips C T,et al.Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses[J].Nature Structural & Molecular Biology,2006,13(1):85-89.
[27]Schouler C,Ehrlich S D,Chopin M C.Sequence and organization of the lactococcal prolate-headed bIL67 phage genome[J].Microbiology,1994,140(11):3061-3069.
[28]Monteville M R,Ardestani B,Geller B L.Lactococcal bacteriophages require a host cell wall carbohydrate and a plasma membrane protein for adsorption and ejection of DNA[J].Applied and Environmental Microbiology,1994,60(9):3204-3211.
[29]Mooney D T,Jann M,Geller B L.Subcellular location of phage infection protein(Pip)in Lactococcus lactis[J].Canadian Journal of Microbiology,2006,52(7):664-672.
[30]Mahony J,Van sinderen D.Structural aspects of the interaction of dairy phages with their host bacteria[J].Viruses,2012,4(9):1410-1424.
[31]Munsch-alatossava P,Alatossava T.The extracellular phage-host interactions involved in the bacteriophage LL-H infection of Lactobacillus delbrueckii ssp.lactis ATCC 15808[J].Frontiers in Microbiology,2013,4:408.
[32]Vinogradov E,Sadovskaya I,Grard T,et al.Structural studies of the cell wall polysaccharide from Lactococcus lactis UC509.9[J].Carbohydrate Research,2018,461:25-31.
[33]Sadovskaya I,Vinogradov E,Courtin P,et al.Another brick in the wall:A rhamnan polysaccharide trapped inside peptidoglycan of Lactococcus lactis[J].MBIO,2017,8(5):e01303-e01317.
[34]Ainsworth S,Sadovskaya I,Vinogradov E,et al.Differences in lactococcal cell wall polysaccharide structure are major determining factors in bacteriophage sensitivity[J].MBIO,2014,5(3):e00814-e00880.
[35]Chapot-chartier M P,Vinogradov E,Sadovskaya I,et al.Cell surface of Lactococcus lactis is covered by a protective polysaccharide pellicle[J].The Journal of Biological Chemistry,2010,285(14):10464-10471.
[36]Farenc C,Spinelli S,Vinogradov E,et al.Molecular insights on the recognition of a Lactococcus lactis cell wall pellicle by thephage 1358 receptor binding protein[J].Journal of Virology,2014,88(12):7005-7015.
[37]Mccabe O,Spinelli S,Farenc C,et al.The targeted recognition of Lactococcus lactis phages to their polysaccharide receptors[J].Molecular Microbiology,2015,96(4):875-886.
[38]Mahony J,Randazzo W,Neve H,et al.Lactococcal 949 group phages recognize a carbohydrate receptor on the host cell surface[J].Applied and Environmental Microbiology,2015,81(10):3299-3305.
[39]Oliveira J,Mahony J,Hanemaaijer L,et al.Biodiversity of bacteriophages infecting Lactococcus lactis starter cultures[J].Journal of Dairy Science,2018,101(1):96-105.
[40]Legrand P,Collins B,Blangy S,et al.The atomic structure of the phage tuc2009 baseplate tripod suggests that host recognition involves two different carbohydrate binding modules[J].MBIO,2016,7(1):e01715-e01781.