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Published on: August 26, 2016
An insect multiligand recognition protein functions as an opsonin for the phagocytosis of microorganisms
Chong Han Kim1, Yong Pyo Shin, Mi Young Noh
1From the Department of Biotechnology, Hoseo University, Asan City, Chungnam 336-795, South Korea.
Abstract:
We characterize a novel pathogen recognition protein obtained from the lepidopteran Galleria mellonella. This protein recognizes Escherichia coli, Micrococcus luteus, and Candida albicans via specific binding to lipopolysaccharides, lipoteichoic acid, and beta-1,3-glucan, respectively. As a multiligand receptor capable of coping with a broad variety of invading pathogens, it is constitutively produced in the fat body, midgut, and integument but not in the hemocytes and is secreted into the hemolymph. The protein was confirmed to be relevant to cellular immune response and to further function as an opsonin that promotes the uptake of invading microorganisms into hemocytes. Our data reveal that the mechanism by which a multiligand receptor recognizes microorganisms contributes substantially to their phagocytosis by hemocytes. A better understanding of an opsonin with the required repertoire for detecting diverse invaders might provide us with critical insights into the mechanisms underlying insect phagocytosis.
Insights
A novel protein from Galleria mellonella acts as a multiligand receptor, recognizing diverse pathogens like bacteria and fungi. This opsonin enhances immune cell phagocytosis, offering insights into insect immunity.
Area of Science:
- Insect immunology
- Invertebrate pathology
- Molecular recognition
Background:
- Pathogen recognition proteins (PRPs) are crucial for innate immunity in invertebrates.
- Galleria mellonella is a key model organism for studying insect immune responses.
Purpose of the Study:
- To characterize a novel multiligand receptor from Galleria mellonella.
- To elucidate the role of this receptor in cellular immune responses and pathogen recognition.
Main Methods:
- Protein isolation and characterization from Galleria mellonella.
- Binding assays to identify pathogen-associated molecular patterns (PAMPs) recognized by the protein.
- Functional assays to assess the protein's role in opsonization and phagocytosis.
Main Results:
- A novel multiligand receptor was identified in Galleria mellonella.
- The protein specifically binds to lipopolysaccharides (LPS) from Escherichia coli, lipoteichoic acid (LTA) from Micrococcus luteus, and beta-1,3-glucan from Candida albicans.
- The receptor is produced in various tissues and secreted into the hemolymph, acting as an opsonin to enhance hemocyte phagocytosis.
Conclusions:
- This multiligand receptor plays a significant role in Galleria mellonella's cellular immunity.
- The recognition mechanism contributes to efficient phagocytosis of diverse microbial invaders.
- Understanding this opsonin provides insights into the broader mechanisms of insect phagocytosis.
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