Characterization of Bacillus phage Gxv1, a novel lytic Salasvirus phage isolated from deep-sea seamount sediments

Author(s):  
Xun Guo ◽  
Tianyou Zhang ◽  
Min Jin ◽  
Runying Zeng
Keyword(s):  
Deep Sea ◽  
BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Oluchi Aroh ◽  
Kenneth M. Halanych

Abstract Background Long Terminal Repeat retrotransposons (LTR retrotransposons) are mobile genetic elements composed of a few genes between terminal repeats and, in some cases, can comprise over half of a genome’s content. Available data on LTR retrotransposons have facilitated comparative studies and provided insight on genome evolution. However, data are biased to model systems and marine organisms, including annelids, have been underrepresented in transposable elements studies. Here, we focus on genome of Lamellibrachia luymesi, a vestimentiferan tubeworm from deep-sea hydrocarbon seeps, to gain knowledge of LTR retrotransposons in a deep-sea annelid. Results We characterized LTR retrotransposons present in the genome of L. luymesi using bioinformatic approaches and found that intact LTR retrotransposons makes up about 0.1% of L. luymesi genome. Previous characterization of the genome has shown that this tubeworm hosts several known LTR-retrotransposons. Here we describe and classify LTR retrotransposons in L. luymesi as within the Gypsy, Copia and Bel-pao superfamilies. Although, many elements fell within already recognized families (e.g., Mag, CSRN1), others formed clades distinct from previously recognized families within these superfamilies. However, approximately 19% (41) of recovered elements could not be classified. Gypsy elements were the most abundant while only 2 Copia and 2 Bel-pao elements were present. In addition, analysis of insertion times indicated that several LTR-retrotransposons were recently transposed into the genome of L. luymesi, these elements had identical LTR’s raising possibility of recent or ongoing retrotransposon activity. Conclusions Our analysis contributes to knowledge on diversity of LTR-retrotransposons in marine settings and also serves as an important step to assist our understanding of the potential role of retroelements in marine organisms. We find that many LTR retrotransposons, which have been inserted in the last few million years, are similar to those found in terrestrial model species. However, several new groups of LTR retrotransposons were discovered suggesting that the representation of LTR retrotransposons may be different in marine settings. Further study would improve understanding of the diversity of retrotransposons across animal groups and environments.


2013 ◽  
Vol 132 ◽  
pp. 178-181 ◽  
Author(s):  
Yin Chen ◽  
Wenjun Mao ◽  
Baofeng Wang ◽  
Lina Zhou ◽  
Qianqun Gu ◽  
...  

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0173750 ◽  
Author(s):  
Ramón Alberto Batista-García ◽  
Thomas Sutton ◽  
Stephen A. Jackson ◽  
Omar Eduardo Tovar-Herrera ◽  
Edgar Balcázar-López ◽  
...  
Keyword(s):  

2021 ◽  
Vol 40 (8) ◽  
pp. 168-175
Author(s):  
Wenlin Wu ◽  
Hongyun Li ◽  
Tiantian Ma ◽  
Xiaobo Zhang

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7624
Author(s):  
Jing-Chang Luo ◽  
Jian Zhang ◽  
Li Sun

Lysozyme is a key effector molecule of the innate immune system in both vertebrate and invertebrate. It is classified into six types, one of which is the goose-type (g-type). To date, no study on g-type lysozyme in crustacean has been documented. Here, we report the identification and characterization of a g-type lysozyme (named LysG1) from the shrimp inhabiting a deep-sea hydrothermal vent in Manus Basin. LysG1 possesses conserved structural features of g-type lysozymes. The recombinant LysG1 (rLysG1) exhibited no muramidase activity and killed selectively Gram-negative bacteria in a manner that depended on temperature, pH, and metal ions. rLysG1 bound target bacteria via interaction with bacterial cell wall components, notably lipopolysaccharide (LPS), and induced cellular membrane permeabilization, which eventually caused cell lysis. The endotoxin-binding capacity enabled rLysG1 to alleviate the inflammatory response induced by LPS. Mutation analysis showed that the bacterial binding and killing activities of rLysG1 required the integrity of the conserved α3 and 4 helixes of the protein. Together, these results provide the first insight into the activity and working mechanism of g-type lysozyme in crustacean and deep-sea organisms.


2006 ◽  
Vol 8 (1) ◽  
pp. 37-49 ◽  
Author(s):  
Tatsunori Nakagawa ◽  
Ken Takai ◽  
Yohey Suzuki ◽  
Hisako Hirayama ◽  
Uta Konno ◽  
...  

2018 ◽  
Vol 118 ◽  
pp. 2176-2184 ◽  
Author(s):  
Zheng-Wen Cai ◽  
Hui-Hua Ge ◽  
Zhi-Wei Yi ◽  
Run-Ying Zeng ◽  
Guang-Ya Zhang
Keyword(s):  

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