Exploring Andean High-Altitude Lake Extremophiles through Advanced Proteotyping

authored by

Katharina Runzheimer, Clément Lozano, Diana Boy, Jens Boy, Roberto Godoy, Francisco J. Matus, Denise Engel, Bruno Pavletic, Stefan Leuko, Jean Armengaud, Ralf Moeller

Abstract

Quickly identifying and characterizing isolates from extreme environments is currently challenging while very important to explore the Earth′s biodiversity. As these isolates may, in principle, be distantly related to known species, techniques are needed to reliably identify the branch of life to which they belong. Proteotyping these environmental isolates by tandem mass spectrometry offers a rapid and cost-effective option for their identification using their peptide profiles. In this study, we document the first high-throughput proteotyping approach for environmental extremophilic and halophilic isolates. Microorganisms were isolated from samples originating from high-altitude Andean lakes (3700-4300 m a.s.l.) in the Chilean Altiplano, which represent environments on Earth that resemble conditions on other planets. A total of 66 microorganisms were cultivated and identified by proteotyping and 16S rRNA gene amplicon sequencing. Both the approaches revealed the same genus identification for all isolates except for three isolates possibly representing not yet taxonomically characterized organisms based on their peptidomes. Proteotyping was able to indicate the presence of two potentially new genera from the families of Paracoccaceae and Chromatiaceae/Alteromonadaceae, which have been overlooked by 16S rRNA amplicon sequencing approach only. The paper highlights that proteotyping has the potential to discover undescribed microorganisms from extreme environments.

Organisation(s)

Institute of Microbiology
Institute of Soil Science

External Organisation(s)

German Aerospace Center (DLR)
Université Paris-Saclay
Universidad Austral de Chile
Universidad de la Frontera

Type

Article

Journal

Journal of proteome research

Volume

23

Pages

891-904

No. of pages

14

ISSN

1535-3893

Publication date

03.2024

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Chemistry(all), Biochemistry

Electronic version(s)

https://doi.org/10.1021/acs.jproteome.3c00538 (Access: Open)