Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition

Tipparat Thiangtrongjit; Onrapak Reamtong; Weerapong Phumratanapraphin; Direk Limmathurotsakul; Surapong Chatpun; Mingkwan Odton; Muthita Vanaporn; Pornpan Pumirat; Usa Boonyuen; Sumate Ampawong; Ngamphol Soonthornworasiri; Poom Adisakwattana; Urai Chaisri; Santi Maneewatchararangsri

doi:10.20944/preprints202210.0099.v1

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preprints.org > biology and life sciences > immunology and microbiology > doi: 10.20944/preprints202210.0099.v1

Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition

Tipparat Thiangtrongjit

Onrapak Reamtong

Weerapong Phumratanapraphin

Direk Limmathurotsakul

Ngamphol Soonthornworasiri

Poom Adisakwattana

Urai Chaisri

Santi Maneewatchararangsri

Version 1 : Received: 30 September 2022 / Approved: 9 October 2022 / Online: 9 October 2022 (02:07:23 CEST)

How to cite: Thiangtrongjit, T.; Reamtong, O.; Phumratanapraphin, W.; Limmathurotsakul, D.; Chatpun, S.; Odton, M.; Vanaporn, M.; Pumirat, P.; Boonyuen, U.; Ampawong, S.; Soonthornworasiri, N.; Adisakwattana, P.; Chaisri, U.; Maneewatchararangsri, S. Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition. Preprints 2022, 2022100099. https://doi.org/10.20944/preprints202210.0099.v1 Thiangtrongjit, T.; Reamtong, O.; Phumratanapraphin, W.; Limmathurotsakul, D.; Chatpun, S.; Odton, M.; Vanaporn, M.; Pumirat, P.; Boonyuen, U.; Ampawong, S.; Soonthornworasiri, N.; Adisakwattana, P.; Chaisri, U.; Maneewatchararangsri, S. Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition. Preprints 2022, 2022100099. https://doi.org/10.20944/preprints202210.0099.v1

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MDPI and ACS Style

Thiangtrongjit, T.; Reamtong, O.; Phumratanapraphin, W.; Limmathurotsakul, D.; Chatpun, S.; Odton, M.; Vanaporn, M.; Pumirat, P.; Boonyuen, U.; Ampawong, S.; Soonthornworasiri, N.; Adisakwattana, P.; Chaisri, U.; Maneewatchararangsri, S. Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition. Preprints 2022, 2022100099. https://doi.org/10.20944/preprints202210.0099.v1

APA Style

Thiangtrongjit, T., Reamtong, O., Phumratanapraphin, W., Limmathurotsakul, D., Chatpun, S., Odton, M., Vanaporn, M., Pumirat, P., Boonyuen, U., Ampawong, S., Soonthornworasiri, N., Adisakwattana, P., Chaisri, U., & Maneewatchararangsri, S. (2022). Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition. Preprints. https://doi.org/10.20944/preprints202210.0099.v1

Chicago/Turabian Style

Thiangtrongjit, T., Urai Chaisri and Santi Maneewatchararangsri. 2022 "Extracellular Secretomes of Leptospira Interrogans Serovar Icterohemorrhagiae Respond to the In Vivo Mimic of Physiological Osmolarity and Temperature Transition" Preprints. https://doi.org/10.20944/preprints202210.0099.v1

Abstract

Leptospirosis remains an important worldwide zoonotic disease caused by Leptospira spp affecting human and animals. This research aims to study the virulent-associated secreted proteins (protein secretome) of pathogenic Leptospira interrogans serovar Icterohemorrhagiae strain RGA (Leptospira RGA) transition from the environment to mammalian physiological osmolarity, temperature (37 °C) and carbon dioxide concentration (5% CO2) conditions for 24 h. Mass Spectrometry and bioinformatics approaches, we identified 69 potential secreted proteins from the culture supernatant of the Leptospira RGA isolate. We discovered transporters and porins such as phosphate porin, outer membrane efflux, ompA family protein, and polymer-forming cytoskeletal family protein under hyperosmotic condition. Under heat stress, degradation enzymes included zinc metallopeptidase, M23 family (LA3456, LA0709), Rhs family protein (LA1765), thermolysin metallopeptidase; / hydrolase family (LA1345, LA2501). Oxidative stress response proteins induced by osmolarity and temperature shifts included chaperon GrpE, DnaK (LA3705), antioxidants, i.e., thiol-specific redoxin, and peroxiredoxin (LA2809). In response to the in vivo transition, metabolic and other enzymes involved in energy production (COG:C), amino acid metabolism and transport (COG:E), and lipid metabolism and transport (COG:I), as well as moonlighting proteins functionally binding to plasminogen and fibronectin and regulating transcription, were also discovered. An overview of secreted proteins will supplement our understanding of Leptospira biology and pathogenesis during infection and also in response to environmental stimuli and their potential virulent determinants have the potential for developing leptospirosis vaccines and diagnosis.

Keywords

Leptospira spp., secretome; virulent-associated secreted proteins; in-vivo mimic mammalian condition

Subject

Biology and Life Sciences, Immunology and Microbiology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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