The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm.

Insect Biochemistry and Molecular Biology
Miao LiMichael R Kanost

Abstract

Members of the serpin superfamily of proteins occur in animals, plants, bacteria, archaea and some viruses. They adopt a variety of physiological functions, including regulation of immune system, modulation of apoptosis, hormone transport and acting as storage proteins. Most members of the serpin family are inhibitors of serine proteinases. In this study, we searched the genome of Manduca sexta and identified 32 serpin genes. We analyzed the structure of these genes and the sequences of their encoded proteins. Three M. sexta genes (serpin-1, serpin-15, and serpin-28) have mutually exclusive alternatively spliced exons encoding the carboxyl-terminal reactive center loop of the protein, which is the site of interaction with target proteases. We discovered that MsSerpin-1 has 14 splicing isoforms, including two undiscovered in previous studies. Twenty-eight of the 32 M. sexta serpins include a putative secretion signal peptide and are predicted to be extracellular proteins. Phylogenetic analysis of serpins in M. sexta and Bombyx mori indicates that 17 are orthologous pairs, perhaps carrying out essential physiological functions. Analysis of the reactive center loop and hinge regions of the protein sequences indicates that 16 of th...Continue Reading

Citations

May 3, 2019·Archives of Insect Biochemistry and Physiology·Muhammad ShakeelFengliang Jin
Sep 10, 2020·Proceedings of the National Academy of Sciences of the United States of America·Yang WangHaobo Jiang
Oct 7, 2020·The FEBS Journal·Catarina NunesTakashi Koyama
Oct 24, 2020·Insect Biochemistry and Molecular Biology·Xiaolong CaoHaobo Jiang
Jan 5, 2022·Archives of Insect Biochemistry and Physiology·Juan D Rios-DíezMaria Goreti de Almeida Oliveira

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