Novel role of the LPS core glycosyltransferase WapH for cold adaptation in the Antarctic bacterium Pseudomonas extremaustralis

PLoS One. 2018 Feb 7;13(2):e0192559. doi: 10.1371/journal.pone.0192559. eCollection 2018.

Abstract

Psychrotroph microorganisms have developed cellular mechanisms to cope with cold stress. Cell envelopes are key components for bacterial survival. Outer membrane is a constituent of Gram negative bacterial envelopes, consisting of several components, such as lipopolysaccharides (LPS). In this work we investigated the relevance of envelope characteristics for cold adaptation in the Antarctic bacterium Pseudomonas extremaustralis by analyzing a mini Tn5 wapH mutant strain, encoding a core LPS glycosyltransferase. Our results showed that wapH strain is impaired to grow under low temperature but not for cold survival. The mutation in wapH, provoked a strong aggregative phenotype and modifications of envelope nanomechanical properties such as lower flexibility and higher turgor pressure, cell permeability and surface area to volume ratio (S/V). Changes in these characteristics were also observed in the wild type strain grown at different temperatures, showing higher cell flexibility but lower turgor pressure under cold conditions. Cold shock experiments indicated that an acclimation period in the wild type is necessary for cell flexibility and S/V ratio adjustments. Alteration in cell-cell interaction capabilities was observed in wapH strain. Mixed cells of wild type and wapH strains, as well as those of the wild type strain grown at different temperatures, showed a mosaic pattern of aggregation. These results indicate that wapH mutation provoked marked envelope alterations showing that LPS core conservation appears as a novel essential feature for active growth under cold conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Antarctic Regions
  • Cold Temperature*
  • Genes, Bacterial
  • Glycosyltransferases / genetics
  • Glycosyltransferases / metabolism*
  • Lipopolysaccharides / metabolism*
  • Pseudomonas / enzymology
  • Pseudomonas / genetics
  • Pseudomonas / physiology*
  • Real-Time Polymerase Chain Reaction

Substances

  • Lipopolysaccharides
  • Glycosyltransferases

Grants and funding

This work was supported by the Agencia Nacional de Promoción Científica y Tecnológica Prestamo BID-PICT 2259. NIL, PMT, ESV; Consejo Nacional de Investigaciones Cientificas y Tecnicas. PIP 2014-2017. NIL. PMT, ESV; Universidad de Buenos Aires.Código 20020130100451BA. NIL, PMT, ESV, FCB and the Agencia Nacional de Promoción Científica y Tecnológica (grant PRH-2013-0017-PICT 2015-0031). LL, ESV and MAC have a graduate student fellowship from CONICET. FCB has an undergraduate student fellowship from UBA. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.