Annotation and expression analysis of cuticular proteins from the tobacco hornworm,Manduca sexta |
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| Affiliation: | 1. Department of Biochemistry and Molecular Biophysics, 141 Chalmers Hall, Kansas State University, Manhattan, KS 66506, USA;2. Department of Entomology, Cornell University, New York State Agricultural Experiment Station, Geneva, NY 14456, USA;3. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA;4. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078, USA;1. Biological and Biomimetic Material Laboratory, Center for Sustainable Materials (SusMat), School of Materials Science and Engineering, Nanyang Technological University (NTU), 50 Nanyang Avenue, Singapore 637553, Singapore;2. School of Biological Sciences, NTU, 60 Nanyang Drive, Singapore 637551, Singapore;3. Bioinformatics Institute, A*STAR, 30 Biopolis Street, #07-01 Matrix, Singapore 138671, Singapore;4. Department of Biological Sciences, National University of Singapore (NUS), 16 Science Drive 4, Singapore 117558, Singapore;5. NTU Institute of Structural Biology, Experimental Medicine Building (EMB), 59 Nanyang Drive, Level 06-01, Singapore 636921, Singapore;1. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA;2. The State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing, 100101, PR China;3. Boyce Thompson Institute, Cornell University, Ithaca, NY, 14853, USA;4. Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA;1. Department of Entomology, Cornell University, New York State Agricultural Experiment Station, Geneva, NY 14456, USA;2. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078, USA;3. Boyce Thompson Institute, Cornell University, Ithaca, NY 14853-1801, USA;4. Department of Biochemistry & Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS 66506, USA;1. School of Plant Protection, Anhui Agricultural University, Hefei, Anhui 230036, PR China;2. Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078, USA;3. Boyce Thompson Institute, Cornell University, Ithaca, NY 14853, USA;4. Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506, USA;5. Division of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA;1. Institut de Recherche sur la Biologie de l''Insecte, UMR CNRS 7261, UFR Sciences et Techniques, Université François-Rabelais, Tours, France;2. Department of Environment and Agrobiotechnologies Centre de Recherche Public – Gabriel Lippmann, Belvaux, Luxembourg;3. Commissariat à l''Energie Atomique et aux Energies Alternatives, Genoscope (Centre National de Séquençage), Evry, France |
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| Abstract: | The insect cuticle is a unique material that covers the exterior of the animal as well as lining the foregut, hindgut, and tracheae. It offers protection from predators and desiccation, defines body shape, and serves as an attachment site for internal organs and muscle. It has demonstrated remarkable variations in hardness, flexibility and elasticity, all the while being light weight, which allows for ease of movement and flight. It is composed primarily of chitin, proteins, catecholamines, and lipids. Proteomic analyses of cuticle from different life stages and species of insects has allowed for a more detailed examination of the protein content and how it relates to cuticle mechanical properties. It is now recognized that several groups of cuticular proteins exist and that they can be classified according to conserved amino acid sequence motifs. We have annotated the genome of the tobacco hornworm, Manduca sexta, for genes that encode putative cuticular proteins that belong to seven different groups: proteins with a Rebers and Riddiford motif (CPR), proteins analogous to peritrophins (CPAP), proteins with a tweedle motif (CPT), proteins with a 44 amino acid motif (CPF), proteins that are CPF-like (CPFL), proteins with an 18 amino acid motif (18 aa), and proteins with two to three copies of a C-X5-C motif (CPCFC). In total we annotated 248 genes, of which 207 belong to the CPR family, the most for any insect genome annotated to date. Additionally, we discovered new members of the CPAP family and determined that orthologous genes are present in other insects. We established orthology between the M. sexta and Bombyx mori genes and identified duplication events that occurred after separation of the two species. Finally, we utilized 52 RNAseq libraries to ascertain gene expression profiles that revealed commonalities and differences between different tissues and developmental stages. |
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| Keywords: | Cuticular proteins Rebers & Riddiford RNAseq Orthology |
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