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Invertebrate-type lysozyme

Yan Liu, Ying-Hao Zhang, Tong Li, Xiao-Tong Cao, Yang Zhou, Jun-Fa Yuan, Ze-Mao Gu, Jiang-Feng Lan
Antimicrobial peptides (AMPs) play important roles in innate immunity against pathogens and lysozymes are a particularly type of AMP. Lysozymes are hydrolytic enzymes that are characterized by their ability to cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, which is the major bacterial cell wall polymer. In this work, a lysozyme was identified from Procambarus clarkii and designated PcLys-i3. Quantitative RT-PCR was used to analyze the tissue distribution and expression profiles of PcLys-i3...
May 31, 2018: Developmental and Comparative Immunology
Hye Young Oh, Chan-Hee Kim, Hye-Jin Go, Nam Gyu Park
Invertebrates, unlike vertebrates which have adaptive immune system, rely heavily on the innate immune system for the defense against pathogenic bacteria. Lysozymes, along with other immune effectors, are regarded as an important group in this defense. An invertebrate-type (i-type) lysozyme, designated Urechis unicinctus invertebrate-type lysozyme, Uu-ilys, has been isolated from nephridia of Urechis unicinctus using a series of high performance liquid chromatography (HPLC), and ultrasensitive radial diffusion assay (URDA) as a bioassay system...
May 9, 2018: Fish & Shellfish Immunology
Tian-Jiang Liao, Jie Gao, Jin-Xing Wang, Xian-Wei Wang
Lysozymes possess antibacterial activities, making them crucial defense proteins in innate immunity. In this study, a chicken-type (c-type) lysozyme (designated PcLyzc) was cloned and characterized from red swamp crayfish Procambarus clarkii. The full-length cDNA had an open reading frame of 435 base pairs encoding a polypeptide of 144 amino acid residues. Multiple alignments and phylogenetic analysis revealed that PcLyzc shared high similarity to the other known invertebrate c-type lysozymes. PcLyzc transcripts were steadily expressed in a wide range of tissues in healthy crayfish, and were prominently up-regulated in the hepatopancreas and gills after Vibrio anguillarum or Aeromonas hydrophila challenge...
August 2018: Developmental and Comparative Immunology
Peng Huang, Jinlei Shi, Qingwen Sun, Xianping Dong, Ning Zhang
Lysozymes are known as ubiquitously distributed immune effectors with hydrolytic activity against peptidoglycan, the major bacterial cell wall polymer, to trigger cell lysis. In the present study, the full-length cDNA sequence of a novel sea urchin Strongylocentrotus purpuratus invertebrate-type lysozyme (sp-iLys) was synthesized according to the codon usage bias of Pichia pastoris and was cloned into a constitutive expression plasmid pPIC9K. The resulting plasmid, pPIC9K-sp-iLys, was integrated into the genome of P...
April 13, 2018: Applied Biochemistry and Biotechnology
Jian Zhou, Shu Zhao, Wen-Hong Fang, Jun-Fang Zhou, Jing-Xiao Zhang, Hongyu Ma, Jiang-Feng Lan, Xin-Cang Li
Lysozymes are widely distributed immune effectors exerting muramidase activity against the peptidoglycan of the bacterial cell wall to trigger cell lysis. However, some invertebrate-type (i-type) lysozymes deficient of muramidase activity still exhibit antimicrobial activity. To date, the mechanism underlying the antimicrobial effect of muramidase-deficient i-type lysozymes remains unclear. Accordingly, this study characterized a novel i-type lysozyme, Splys-i, in the mud crab Scylla paramamosain. Splys-i shared the highest identity with the Litopenaeus vannamei i-type lysozyme (Lvlys-i2, 54% identity) at the amino acid level...
September 2017: Developmental and Comparative Immunology
Dinglong Yang, Qing Wang, Ruiwen Cao, Lizhu Chen, Yongliang Liu, Ming Cong, Huifeng Wu, Fei Li, Chenglong Ji, Jianmin Zhao
Lysozymes play an important role in the innate immune responses with which mollusks respond to bacterial invasion through its lytic activity. In the present study, two c-type lysozymes (designed as VpCLYZ-1 and VpCLYZ-2, respectively) were identified and characterized from the manila clam Venerupis philippinarum. The full-length cDNA of VpCLYZ-1 and VpCLYZ-2 was of 629 and 736 bp, encoding a polypeptide of 156 and153 amino acid residues, respectively. The deduced amino acid sequences of VpCLYZs showed high similarity to other known invertebrate c-type lysozymes...
August 2017: Developmental and Comparative Immunology
Jiefeng Gao, Hongliang Zuo, Linwei Yang, Jian-Hui He, Shengwen Niu, Shaoping Weng, Jianguo He, Xiaopeng Xu
Cyanobacteria are ubiquitously distributed in water on the Earth. It has long been known that the cyanobacterial bloom in aquaculture ponds can cause acute and massive deaths of shrimp. However, the long-term and chronic effects of the cyanobacterial bloom on shrimp are still poorly understood. In this study, the immune state of white pacific shrimp, Litopenaeus vannamei, surviving a naturally occurring cyanobacterial bloom was investigated and tracked for 70 d. Compared with the control, the growth of shrimp suffering high concentrations of cyanobacteria was obviously postponed...
February 2017: Fish & Shellfish Immunology
Courtney E Hart, Michael J Lauth, Cassidy S Hunter, Brennan R Krasny, Kristin M Hardy
The xenoestrogen 4-nonylphenol (NP) is a ubiquitous aquatic pollutant and has been shown to impair reproduction, development, growth and, more recently, immune function in marine invertebrates. We investigated the effects of short-term (7 d) exposure to low (2 μg l(-1)) and high (100 μg l(-1)) levels of NP on cellular and humoral elements of the innate immune response of Crassostrea gigas to a bacterial challenge. To this end, we measured 1) total hemocyte counts (THC), 2) relative transcript abundance of ten immune-related genes (defh1, defh2, bigdef1, bigdef2, bpi, lysozyme-1, galectin, C-type lectin 2, timp, and transglutaminase) in the hemocytes, gill and mantle, and 3) hemolymph plasma lysozyme activity, following experimental Vibrio campbellii infection...
November 2016: Fish & Shellfish Immunology
Maria João Gravato-Nobre, Filipa Vaz, Sergio Filipe, Ronald Chalmers, Jonathan Hodgkin
Little is known about the relative contributions and importance of antibacterial effectors in the nematode C. elegans, despite extensive work on the innate immune responses in this organism. We report an investigation of the expression, function and regulation of the six ilys (invertebrate-type lysozyme) genes of C. elegans. These genes exhibited a surprising variety of tissue-specific expression patterns and responses to starvation or bacterial infection. The most strongly expressed, ilys-3, was investigated in detail...
August 2016: PLoS Pathogens
Yoshito Abe, Mitsuru Kubota, Shinya Takazaki, Yuji Ito, Hiromi Yamamoto, Dongchon Kang, Tadashi Ueda, Taiji Imoto
Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEL) mutant was designed by introducing the substituted catalytic residue Asp46 or Glu46, respectively, based on Venerupis philippinarum (Vp) lysozyme structure as a representative of invertebrate-type (i-type) lyzozyme. These mutations restored the bell-shaped pH-dependency of the enzyme activity from the sigmoidal pH-dependency observed for the Asp52Ser mutant. Furthermore both lysozyme mutants possessed retaining mechanisms like Vp lysozyme and HEL...
September 2016: Protein Science: a Publication of the Protein Society
Ting Chen, Chunhua Ren, Yanhong Wang, Peng Luo, Xiao Jiang, Wen Huang, Chang Chen, Chaoqun Hu
The full-length cDNA coding for a novel invertebrate (i-type) lysozyme was identified in Pacific white shrimp (Litopenaeus vannamei). The newly obtained L. vannamei lysozyme is similar to the Penaeus monodon i-type lysozyme 2, but it is distant from the known L. vannamei c-type lysozyme and i-type lysozyme 1 in protein sequence; therefore, it was defined as L. vannamei i-type lysozyme 2 (lyz-i2). Expression of L. vannamei lyz-i2 transcripts were ubiquitously detected in all tissues we selected, with the highest abundance observed in the hemolymph...
July 2016: Fish & Shellfish Immunology
Keiichiro Koiwai, Rod Russel R Alenton, Hidehiro Kondo, Ikuo Hirono
In invertebrates, hemocytes play an important role in immune responses. Recently, a novel form of innate immune mechanism called extracellular traps (ETs) was identified in shrimps, where DNA and antimicrobial peptides form complex structure to entrap the invading microbes. In this study, we detected the formation of ETs from hemocytes of kuruma shrimp in response to various stimulations, including phorbol myristate acetate (PMA), lipopolysaccharide (LPS), peptidoglycan (PGN) and Escherichia coli. E. coli cells were also found to be trapped by ET fibers...
May 2016: Fish & Shellfish Immunology
Ewa Gajda, Gabriela Bugla-Płoskońska
Lysozyme (LZ, muramidase, N-acetylmuramylhydrolase) is a protein occuring in animals, plants, bacteria and viruses. It can be found e.g. in granules of neutrophils, macrophages and in serum, saliva, milk, honey and hen egg white. The enzyme hydrolyzes the β-1,4 glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) of cell wall peptidoglycan (PG) in Gram-positive and Gram-negative bacteria. In the animal kingdom, three muramidase types have been identified: the c-type (chicken type), the g-type (goose-type) and the i-type (invertebrates)...
2014: Postȩpy Higieny i Medycyny Doświadczalnej
Kazutaka Yokoyama, Michihiko Sato, Toshihiro Haneda, Kentaro Yamazaki, Takashi Kitano, Kazuo Umetsu
PFA (Phalera flavescens agglutinin) lectin purified from larvae of the lobster moth (P. flavescens) shows a strong binding ability specific to the N-acetyllactosamine (Galβ1-4GlcNAc) site. We determined the genomic and cDNA sequences of the PFA gene, which consists of five exons and spans approximately 5 kb of a genomic region. Surprisingly, the amino acid sequence (149 amino acids) was similar to invertebrate-type lysozymes and related proteins. The predicted tertiary structure of the PFA protein was similar to the lysozymes of clams such as the common orient clam (Meretrix lusoria) and Japanese littleneck (Venerupis philippinarum (Tapes japonica))...
November 2014: Insect Biochemistry and Molecular Biology
Na Xu, Junli Pan, Shousheng Liu, Qinggang Xue, Shicui Zhang
The lysozymes identified so far in animals belong to the g-type, c-type, and i-type. Vertebrate animals possess only the former two types, i.e., g- and c-types, while all the three types have been reported in invertebrates. Here we demonstrate that (1) three cDNAs that encode g-, c-, and i-type lysozymes, respectively, were identified in a single species of the amphioxus Branchiostoma japonicum; (2) all the 3-type genes displayed distinct tissue-specific expression pattern; (3) recombinant g-, c-, and i-type lysozymes all exhibited enzymatic activities; and (4) native g-, c-, and i-type lysozymes were identified in the different tissues of amphioxus...
October 2014: Developmental and Comparative Immunology
Francesco Buonocore, Elisa Randelli, Pamela Trisolino, Angelo Facchiano, Donatella de Pascale, Giuseppe Scapigliati
In fish, the first line of defense is represented by the innate immune system and the lysozyme is one of the molecules involved in this mechanism of protection. Three types of lysozymes have been identified in metazoan, the c-type (chicken or conventional), the g-type (goose-type) and the i-type (invertebrate type). They are all involved in the hydrolysation of the bacterial cell wall. Our work has been focused on the molecular characterization, expression analysis by real-time PCR, both at basal condition and after in vivo challenges, and 3D structural studies on the g-type lysozyme from sea bass (Dicentrarchus labrax L...
November 2014: Molecular Immunology
Viswanathan Karthik, Vijayan Kamalakannan, Ancy Thomas, Naduvilamuriparambu Saidumuhammed Sudheer, Issac S Bright Singh, Rangarajan Badri Narayanan
Lysozyme gene from Fenneropenaeus indicus was cloned, expressed in Escherichia coli and characterized. The cDNA consists of 477 base pairs and encodes amino acid sequence of 159 residues. F. indicus lysozyme had high identity (98%) with Fenneropenaeus merguiensis and Fenneropenaeus chinensis and exhibits low to moderate identities with lysozymes of other invertebrates and vertebrates. This lysozyme is presumed to be chicken types as it possesses two catalytic and eight cysteine residues that are conserved across c-type lysozymes and a c-terminal extension, which is a characteristic of lysozymes from marine invertebrates...
June 2014: Probiotics and Antimicrobial Proteins
Yuko Kuwano, Kazunari Yoneda, Yuya Kawaguchi, Norie Araki, Tomohiro Araki
To determine the structure and functional relationships of invertebrate lysozymes, we isolated a new invertebrate (i)-type lysozyme from the common orient clam (Meretrix lusoria) and determined the complete amino acid sequence of two isozymes that differed by one amino acid. The determined sequence showed 65% similarity to a lysozyme from Venerupis philippinarum (Tapes japonica), and it was therefore classified as an i-type lysozyme. The lytic activities of this lysozyme were similar to those of previously reported bivalve i-type lysozymes, but unlike the V...
2013: Bioscience, Biotechnology, and Biochemistry
Yuko Kuwano, Kazunari Yoneda, Yuya Kawaguchi, Tomohiro Araki
To evaluate the structure-function relationships of invertebrate lysozymes, a new invertebrate-type (i-type) lysozyme was isolated from the common orient clam (Meretrix lusoria) and the tertiary structure of this enzyme was determined. Comparison of the tertiary structure of this enzyme with those of chicken and Venerupi philippinarum lysozymes revealed that the location of the side chain of the second catalytic residue, an aspartic acid, and the N-acetylglucosamine trimer bound at subsites A-C were different...
November 2013: Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Nichole Hinds Vaughan, Sylvia L Smith
Lysozyme is a ubiquitous antibacterial enzyme that occurs in numerous invertebrate and vertebrate species. Three forms have been described c-type, g-type and i-type which differ in primary structure. Shark lysozyme has not been characterized; here we report on the isolation and characterization of lysozyme from unstimulated shark (Ginglymostoma cirratum) leukocytes and provide amino acid sequence data across the highly conserved active site of the molecule identifying it to be a c-type lysozyme. A leukocyte lysate was applied either (a) to the first of two sequential DE-52 cellulose columns or alternatively, (b) to a DEAE-Sepharose column...
December 2013: Fish & Shellfish Immunology
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