Best AM et al. (2018) Cell Microbiol "Evasion of phagotrophic predation by protist hosts and innate immunity of metazoan hosts by Legionella pneumophilla."

Best AM, Kwaik YA

[Cell Microbiol, 2018]

Legionella pneumophila is a ubiquitous environmental bacterium that has evolved to infect and proliferate within amoebae and other protists. It is thought that accidental inhalation of contaminated water particles by humans is what has enabled this pathogen to proliferate within alveolar macrophages and cause pneumonia. However, the highly evolved macrophages are equipped more sophisticated innate defense mechanisms than protists, such as the evolution of phagotrophic feeding into phagocytosis with more evolved innate defense processes. Not surprisingly, the majority of proteins involved in phagosome biogenesis (~80%) have origins in the phagotrophy stage of evolution. There are a plethora of highly evolved cellular and innate metazoan processes, not represented in Protist biology, that are modulated by L. pneumophila; including TLR2 signaling, NF-B, apoptotic and inflammatory processes, histone modification, caspases, and the NLRC-Naip5 inflammasomes. Importantly, L. pneumophila infects hemocytes of the invertebrate Galleria mellonella, kill G. mellonella larvae, and proliferate in and kill Drosophila adult flies and Caenorhabditis elegans. Although co-evolution with protist hosts has provided a substantial blueprint for L. pneumophila to infect macrophages, we discuss the further evolutionary aspects of co-evolution of L. pneumophila and its adaptation to modulate various highly evolved innate metazoan processes prior to becoming a human pathogen.

adrenomedullin binding

Binding to adrenomedullin (AM).

KAN2958

Caenorhabditis elegans

KAN3314

Caenorhabditis elegans

KAN2869

Caenorhabditis elegans

KAN2870

Caenorhabditis elegans

KAN2842

Caenorhabditis elegans

WBsf981139

Caenorhabditis elegans

ATFS-1 binding site near 'C37A5.7', 'best-8'.

Kim, Jimin et al. (2021) International Worm Meeting "Identify the function of calcium-activated chloride channel Bestrophin in C. elegans"

Kim, Kyuhyung, Kim, Seoyeong, Kim, Jimin

[International Worm Meeting, 2021]

Bestrophin is a calcium-activated chloride channel of which gene family is identified in many organisms. In humans, bestrophins are encoded by the four genes; BEST1-4. BEST channels are expressed in multiple tissues and appear to mediate diverse functions, including cell volume regulation (Fischmeister & Hartzell, 2005; Milenkovic et al., 2015). For example, BEST-1 gene is expressed in the retinal pigment epithelium (RPE), and BEST-1 mutation is associated with a variety of eye diseases, including best vitelliform macular dystrophy (BVMD) (Marquardt et al., 1998; Petrukhin et al., 1998). However, the exact functions of the bestrophins have not been identified. C. elegans has 26 genes of bestrophin (best-1 to 26), of which expression patterns and functions remain largely unknown. To investigate the expression patterns of best genes in C. elegans, we expressed a green fluorescent protein (GFP) under the control of the promoter of each best gene. We found that these genes are expressed in most, but not all, cell types, including intestine, muscle, hypodermal and neuronal cells. For example, best-3 and best-4 genes are expressed in an excretory cell, which has been implicated in osmoregulation. We are also characterizing nine mutants, including best-3 and best-4. Furthermore, we plan to perform electrophysiology using the best cDNAs to examine physiological characteristics of the C. elegans BEST channels.

transcript: ZK675.3b [Browse genome (BioProject PRJNA13758)]

Caenorhabditis elegans

non-coding Transcript Isoform