Identification and genome analysis of a novel 17β-estradiol degradation bacterium, Lysinibacillus sphaericus DH-B01

Horizontal transfer of large plasmid with type IV secretion system and mosquitocidal genomic island with excision and integration capabilities in Lysinibacillus sphaericus

“…The chromosome sequences of 1593 (CP064068), SSII‐1 (CP064070), and KellenQ (CP064067) obtained in this study were compared with all other L. sphaericus genomes published (up to December 2020), including C3‐41 (NC_010382.1), 2362 (CP015224.1), OT4b.25 (CP014643.1), III(3)7 (CP014856.1), DH‐B01 (CP045583), and DSM 28 (NZ_CP019980) (Hu et al ., 2008; Hernandez‐Santana et al ., 2016; Rey et al ., 2016a, b; Wang et al ., 2020). Those isolates with high larvicidal activity (e.g., C3‐41, 2362, OT4b.25, III(3)7, and 1593) were conserved, whereas avirulent isolates (e.g., DH‐B01 and DSM 28) were diverse.…”

Experimental and Genomic Evaluation of the Oestrogen Degrading Bacterium Rhodococcus equi ATCC13557

“…DSSKY-A-001 and these were expressed in the presence of E2 relative to a control, the dehydrogenase likely converting E2 to E1 and dioxygenase carrying out oxygenation to further metabolise E1 ( Qiu et al, 2019 ). The degradation pathway of L. sphaericus DH-B01 was postulated in which the enzyme dehydrogenase was suggested to be responsible for the conversion of E2 to E1, dioxygenase for A ring cleavage, oxygenase may be responsible for the conversion of 4-hydroxyl-E1 and B ring cleavage ( Wang Y. et al, 2020 ). S. maltophilia SJTL3 also contained genes coding for the oestrogen degradation enzymes, dioxygenase, 3/17β-hydroxysteroid dehydrogenase, acyl-CoA dehydrogenase, and alcohol dehydrogenase these are likely to carry out the oxidation of the A ring, dehydrogenation of the D ring, degradation of E1 by the lactone pathway, and ketonisation, respectively ( Lee and Liu, 2002 ; Kurisu et al, 2010 ; Yu et al, 2016 ; Xiong et al, 2020 ).…”

“…Furthermore, several other genes encoding the enzymes potentially involved in oestrogen degradation were identified in the genome of the same strain (e.g., phenol hydroxylase, alkane oxygenase, short-chain dehydrogenase, catechol 2,3-dioxygenase, acetyl-CoA-acetyltransferase, and enoyl-CoA hydratase) ( Qiu et al, 2019 ). Wang Y. et al (2020) predicted 159 dehydrogenases, 9 monooxygenase, 6 dioxygenase, 16 hydratase, and 27 hydrolase encoding genes within the genome of the E2-degrader, Lysinibacillus sphaericus DH-B01. Genes encoding cholesterol oxidase, steroid Δ-isomerase, cytochrome P450 monooxygenase, 3δ-steroid-1-dehydrogenase, 3-steroid-9α-hydroxylase (KSH), and 3α,20β-hydroxysteroid steroid dehydrogenase were identified within the genome of the E1-degrading Rhodococcus sp.…”

“…DSSKY-A-001, Novosphingobium sp. ES2-1, and L. sphaericus DH-B01, the first step in the degradation of E2 appears to be the oxidation of the C-17 hydroxyl position by an SDR such as 17β-hydroxysteroid dehydrogenase to produce E1 ( Hu et al, 2011 ; Qin et al, 2016 ; Zheng et al, 2016 ; Chen et al, 2017 ; Ye et al, 2017 ; Xiong et al, 2018 , 2020 ; Qiu et al, 2019 ; Wang et al, 2019 ; Wu et al, 2019 ; Wang Y. et al, 2020 ; Li et al, 2021 ). However, there are examples of different E2 degradation pathways reported in bacteria, such as hydroxylation at different positions within different saturated rings (B, C, or D) to produce 4-hydroxyestradiol (4-OH-E2), keto-E1, keto-E2, or E3 ( Xuan et al, 2008 ; Kurisu et al, 2010 ; Yu et al, 2013 ).…”

“…However, there are examples of different E2 degradation pathways reported in bacteria, such as hydroxylation at different positions within different saturated rings (B, C, or D) to produce 4-hydroxyestradiol (4-OH-E2), keto-E1, keto-E2, or E3 ( Xuan et al, 2008 ; Kurisu et al, 2010 ; Yu et al, 2013 ). For Sphingomonas strain KC8 and L. sphaericus DH-B01, E1 is suggested to be further degraded by A ring hydroxylation by monooxygenase to produce 4-hydroxy oestrone (4-OH-E1), followed by A ring cleavage by dioxygenase ( Chen et al, 2017 ; Wang Y. et al, 2020 ). Although in E1 degradation by Acinetobacter sp.…”