The fruit fly forms a magnificent model for interpreting conserved host innate immune signaling and functional processes in response to microbial assaults. In the broad research field of host-microbe interactions, model hosts are used in conjunction with a variety of pathogenic microorganisms to disentangle host immune system activities and microbial pathogenicity strategies. The pathogen is considered an established model for analyzing bacterial virulence and symbiosis due to its unique life cycle that extends between two invertebrate hosts: an insect and a parasitic nematode. In recent years, particular focus has been given to the mechanistic participation of the thioester-containing proteins (TEPs) in the overall immune capacity of the fly upon response against the pathogen alone or in combination with its specific nematode vector . The original role of certain TEPs in the insect innate immune machinery was linked to the antibacterial and antiparasite reaction of the mosquito malaria vector ; however, revamped interest in the immune competence of these molecules has recently emerged from the - infection system. Here, we review the latest findings on this topic with the expectation that such information will refine our understanding of the evolutionary immune role of TEPs in host immune surveillance.
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http://dx.doi.org/10.3390/insects11020085 | DOI Listing |
Insect Biochem Mol Biol
January 2025
Jiangsu Key Laboratory of Infection and Immunity, MOE Key Laboratory of Geriatric Diseases and Immunology, The Forth Affiliated Hospital of Soochow University, Institutes of Biology and Medical Sciences, Suzhou Medical College of Soochow University, Suzhou, China. Electronic address:
Disease vectors, such as arthropods, primarily rely on innate immunity to counteract pathogen invasions, typically through the recognition and binding of pathogen-associated molecular patterns (PAMPs) by the host's pattern recognition receptors (PRRs). As a conserved immune effector gene family from insects to mammals, the complement system may play an essential role in combating pathogenic microorganisms. In arthropods, the complement proteins are often referred to as thioester-containing proteins (TEPs) because thioester motifs are one of the essential functional domains of the first proteins characterized within the C3 and AM family.
View Article and Find Full Text PDFPLoS One
October 2024
Faculty of Health Sciences, School of Medical Laboratory Sciences, Jimma University, Jimma, Ethiopia.
Chem Pharm Bull (Tokyo)
July 2024
Faculty of Pharamaceutical Sciences, Niigata University of Pharmacy and Medical and Life Sciences.
We report two methods for the preparation of peptide thioesters containing Tyr(SOH) residue(s), without use of a protecting group for the sulfate moiety. The first was based on direct thioesterification using carbodiimide on a fully protected peptide acid, prepared on a 2-chlorotrityl (Clt) resin with fluoren-9-ylmethoxycarbonyl (Fmoc)-based solid-phase peptide synthesis (Fmoc-SPPS). Subsequent deprotection of the protecting groups with trifluoroacetic acid (TFA) (0 °C, 4 h) yielded peptide thioesters containing Tyr(SOH) residue(s).
View Article and Find Full Text PDFJ Med Chem
June 2024
AbbVie Bioresearch Center, 381 Plantation Street, Worcester, Massachusetts 01605, United States.
Fish Shellfish Immunol
February 2024
State Key Laboratory of Mariculture Breeding, Fujian Agriculture and Forestry University, Fuzhou, 350002, China; Key Laboratory of Marine Biotechnology of Fujian Province, Institute of Oceanology, Fujian Agriculture and Forestry University, Fuzhou, 350002, China. Electronic address:
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