Unravelling the Biological Functions of Photorhabdus Lectins: Insights into Pathogenicity and Symbiotic Relationships

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F24%3A00139672" target="_blank" >RIV/00216224:14310/24:00139672 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Unravelling the Biological Functions of Photorhabdus Lectins: Insights into Pathogenicity and Symbiotic Relationships

Popis výsledku v původním jazyce

Photorhabdus spp., a bacteria known for its symbiotic relationship with nematodes of genus Heterorhabditis and its pathogenicity towards insects, produces a variety of lectins that are considered to play significant roles in its life cycle. Our research focuses on identifying and characterising these bacterial lectins, specifically the PLL family and two newly discovered proteins, PLU1 and PluLec. These lectins have been structurally analysed to understand their molecular architecture and suggest their potential biological functions. The PLL family includes five homologous lectins identified in P. laumondii with a preference for fucosylated glycans. PLLs were shown to participate in Photorhabdsus virulence rather than supporting its interaction with the nematode host. Similarly to PLLs, PLU1 belongs to fucose-binding lectins and was observed to bind to the nematode’s inner tissues, suggesting the diverse biological roles of these proteins. PluLec, on the other hand, is a galactose-binding protein identified in Photorhabdus as a homolog of the PA-IL lectin from the human opportunistic pathogen Pseudomonas aeruginosa, where it serves as an important virulence factor. Notably, PluLec increases the mortality of Drosophila adults after injection, highlighting its significant role in enhancing bacterial virulence. We hypothesise that Photorhabdus lectins are integral to bacterial pathogenicity, facilitating the evasion of insect defenses and disrupting normal immune responses. Additionally, the involvement of studied lectins in mutualism is being explored. Lectins may aid in establishing and maintaining the symbiotic relationship between Photorhabdus and its nematode host by mediating cell-cell interactions and signalling processes. Overall, our research provides new insights into the structural and functional diversity of bacterial lectins in Photorhabdus spp. By elucidating the roles of PLLs, PLU1, and PluLec, we aim to better understand the complex interactions that underpin Photorhabdus pathogenicity, mutualism, and intra-population dynamics. This knowledge could lead to novel strategies for managing Photorhabdus-related infections and leveraging its symbiotic properties for biocontrol applications. This research was supported by the Grant Agency of the Czech Republic, project No. GAČR 23-06457S.

Název v anglickém jazyce

Unravelling the Biological Functions of Photorhabdus Lectins: Insights into Pathogenicity and Symbiotic Relationships

Popis výsledku anglicky

Photorhabdus spp., a bacteria known for its symbiotic relationship with nematodes of genus Heterorhabditis and its pathogenicity towards insects, produces a variety of lectins that are considered to play significant roles in its life cycle. Our research focuses on identifying and characterising these bacterial lectins, specifically the PLL family and two newly discovered proteins, PLU1 and PluLec. These lectins have been structurally analysed to understand their molecular architecture and suggest their potential biological functions. The PLL family includes five homologous lectins identified in P. laumondii with a preference for fucosylated glycans. PLLs were shown to participate in Photorhabdsus virulence rather than supporting its interaction with the nematode host. Similarly to PLLs, PLU1 belongs to fucose-binding lectins and was observed to bind to the nematode’s inner tissues, suggesting the diverse biological roles of these proteins. PluLec, on the other hand, is a galactose-binding protein identified in Photorhabdus as a homolog of the PA-IL lectin from the human opportunistic pathogen Pseudomonas aeruginosa, where it serves as an important virulence factor. Notably, PluLec increases the mortality of Drosophila adults after injection, highlighting its significant role in enhancing bacterial virulence. We hypothesise that Photorhabdus lectins are integral to bacterial pathogenicity, facilitating the evasion of insect defenses and disrupting normal immune responses. Additionally, the involvement of studied lectins in mutualism is being explored. Lectins may aid in establishing and maintaining the symbiotic relationship between Photorhabdus and its nematode host by mediating cell-cell interactions and signalling processes. Overall, our research provides new insights into the structural and functional diversity of bacterial lectins in Photorhabdus spp. By elucidating the roles of PLLs, PLU1, and PluLec, we aim to better understand the complex interactions that underpin Photorhabdus pathogenicity, mutualism, and intra-population dynamics. This knowledge could lead to novel strategies for managing Photorhabdus-related infections and leveraging its symbiotic properties for biocontrol applications. This research was supported by the Grant Agency of the Czech Republic, project No. GAČR 23-06457S.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA23-06457S" target="_blank" >GA23-06457S: Identifikace a funkční charakteristika bioaktivních molekul produkovaných entomopatogenními hlísticemi</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů