An N-acetyllactosamine-specific lectin,PFA, isolated from a moth (Phalera flavescens), structurally resembles an invertebrate-type lysozyme |
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| Institution: | 1. Department of Biomolecular Functional Engineering, College of Engineering, Ibaraki University, 4-12-1 Nakanarusawa-cho, Hitachi 316-8511, Japan;2. Technical Support Center of Education and Research, Yamagata University School of Medicine, 2-2-2 Iidanishi, Yamagata 990-9585, Japan;3. Department of Forensic Medicine, Yamagata University School of Medicine, 2-2-2 Iidanishi, Yamagata 990-9585, Japan;1. Department of General Practice, First Affiliated Hospital, Zhejiang University School of Medicine, The Key Laboratory of Infectious Diseases, Hangzhou 310003, China;2. The State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, First Affiliated Hospital, Zhejiang University School of Medicine, The Key Laboratory of Infectious Diseases, Hangzhou 310003, China;3. Huzhou Teachers College, Huzhou 313000, China;4. Center of Disease Control and Prevention, Hangzhou 310052, China;1. Spine Unit, Department of Orthopaedic Surgery, Rigshospitalet, University of Copenhagen, Nørregade 10, 1165 København, Denmark;2. Department of Orthopedics and Scoliosis Surgery, Texas Children''s Hospital, TX, USA;1. Department of Animal and Veterinary Sciences, Clemson University, Clemson, South Carolina, USA;2. Department of Animal Science, University of Tennessee, Knoxville, Tennessee, USA;1. Faculty of Chemistry, Department of Science and Humanities, Dr. Mahalingam College of Engineering and Technology (Dr. MCET), Udumalai Road, Pollachi 642 003, Tamil Nadu, India;2. Department of Chemistry, Manonmaniam Sundaranar University, Tirunelveli 627 012, Tamil Nadu, India;3. Department of Chemistry, Texas A&M University, College Station, TX 77842, USA;1. Center for Fisheries, Aquaculture and Aquatic Sciences and Department of Zoology, Southern Illinois University, Carbondale, IL 62901, USA;2. Biology and Environmental Studies, Alma College, Alma, MI 48801, USA |
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| Abstract: | 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)). The PFA, however, lacks a catalytically essential amino acid, an Asp (D), which is one of the two important amino acids (Glu (E) and D) express the function of lysozyme. As a result, lysozyme activity assays indicated that PFA does not have lysozyme activity. Results suggest that the PFA gene evolved from a lysozyme gene through the loss of lysozyme activity sites and the acquisition of lectin activity during evolution of the genus Phalera. |
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| Keywords: | Lectin Lobster moth Lysozyme Gene Evolution |
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