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A tick C1q protein alters infectivity of the Lyme disease agent by modulating interferon γ

ABSTRACT: A tick C1q protein alters infectivity of the Lyme disease agent by modulating interferon γ

PROVIDER: PRJNA854660 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19912341_1.fastq.gz	Fastqsanger.gz
	SRR19912341_2.fastq.gz	Fastqsanger.gz
	SRR19912342_1.fastq.gz	Fastqsanger.gz
	SRR19912342_2.fastq.gz	Fastqsanger.gz
	SRR19912343_1.fastq.gz	Fastqsanger.gz

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A tick C1q protein alters infectivity of the Lyme disease agent by modulating interferon γ

Project description:To understand the immunomodulation roles of complement C1q-like protein 3 (IsC1ql3), we utilized RNA sequencing (RNA-seq) to investigate the effect of IsC1ql3 on the murine transcriptome.

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A tick C1q protein alters infectivity of the Lyme disease agent by modulating interferon γ.

Project description:In North America, the Lyme disease agent, Borrelia burgdorferi, is commonly transmitted by the black-legged tick, Ixodes scapularis. Tick saliva facilitates blood feeding and enhances pathogen survival and transmission. Here, we demonstrate that I. scapularis complement C1q-like protein 3 (IsC1ql3), a tick salivary protein, directly interacts with B. burgdorferi and is important during the initial stage of spirochetal infection of mice. Mice fed upon by B. burgdorferi-infected IsC1ql3-silenced ticks, or IsC1ql3-immunized mice fed upon by B. burgdorferi-infected ticks, have a lower spirochete burden during the early phase of infection compared with control animals. Mechanically, IsC1ql3 interacts with the globular C1q receptor present on the surface of CD4+ and CD8+ T cells, resulting in decreased production of interferon γ. IsC1ql3 is a C1q-domain-containing protein identified in arthropod vectors and has an important role in B. burgdorferi infectivity as the spirochete transitions from the tick to vertebrate host.

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Tick Adiponectin Receptor-Mediated Phospholipid Metabolism Contributes to Borrelia burgdorferi Colonization

Project description:Adiponectin-mediated pathways contribute to mammalian homeostasis; however, little is known about adiponectin and adiponectin receptor signaling in arthropods. In this study, we demonstrate that Ixodes scapularis ticks have an adiponectin receptor-like protein (ISARL) but lack adiponectin, suggesting activation by alternative pathways. ISARL expression is significantly upregulated in the tick gut after Borrelia burgdorferi infection, suggesting that ISARL signaling may be co-opted by the Lyme disease agent. Consistent with this, RNA interference (RNAi)-mediated silencing of ISARL significantly reduced the B. burgdorferi burden in the tick. RNA-seq-based transcriptomics and RNAi assays demonstrate that ISARL-mediated phospholipid metabolism by phosphatidylserine synthase I is associated with B. burgdorferi survival. Furthermore, the tick complement C1q-like protein 3 interacts with ISARL, and B. burgdorferi facilitates this process. This study identifies a new tick metabolic pathway that is connected to the life cycle of the Lyme disease spirochete.

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