ArticleInsect biochemistry and molecular biology2019
The three-dimensional structure and recognition mechanism of Manduca sexta peptidoglycan recognition protein-1.
Article in Insect biochemistry and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Insect immunity unveiled: exploring the molecular and cellular defenses against microbial threats.Archives of microbiology · 2026Review
- Pattern recognition, hemolymph protease-14 activation, and enhancement of lysozyme-mediated bacteria killing by soluble peptidoglycan recognition proteins in Manduca sexta.Insect biochemistry and molecular biology · 2025Article
- An evolutionarily conserved serine protease network mediates melanization and Toll activation inScience advances · 2023Article
- Preferential binding of DAP-PGs by major peptidoglycan recognition proteins found in cell-free hemolymph of Manduca sexta.Insect biochemistry and molecular biology · 2022Article
- Ligand recognition by peptidoglycan recognition protein-S (PGRP-S): structure of the complex of camel PGRP-S with heptanoic acid at 2.15 Å resolution.International journal of biochemistry and molecular biology · 2022Article
- A Short-Type Peptidoglycan Recognition Protein 1 (PGRP1) Is Involved in the Immune Response in Asian Corn Borer,International journal of molecular sciences · 2021Article
- Changes in composition and levels of hemolymph proteins during metamorphosis of Manduca sexta.Insect biochemistry and molecular biology · 2020Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Peptidoglycan recognition proteins (PGRPs) recognize bacteria through their unique cell wall constituent, peptidoglycans (PGs). PGRPs are conserved from insects to mammals and all function in antibacterial defense. In the tobacco hornworm Manduca sexta, PGRP1 and microbe binding protein (MBP) interact with PGs and hemolymph protease-14 precursor (proHP14) to yield active HP14. HP14 triggers a serine protease network that produces active phenoloxidase (PO), Spätzle, and other cytokines to stimulate immune responses. PGRP1 binds preferentially to diaminopimelic acid (DAP)-PGs of Gram-negative bacteria and Gram-positive Bacillus and Clostridium species than Lys-PGs of other Gram-positive bacteria. In this study, we synthesized DAP- and Lys-muramyl pentapeptide (MPP) and monitored their associations with M. sexta PGRP1 by surface plasmon resonance. The K
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