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Guevara-Hernandez, E.

Publications and source records attributed to Guevara-Hernandez, E..

2 recordsLinked to original sources

Biofilm formation and maize root-colonization of seed-endophytic Bacilli isolated from native maize landraces

Agricultural microbiology seeks to replace the use of agrochemicals with microbe-based products. Plant growth-promoting bacteria (PGPB) are often selected based on their functions in vitro, and then, their effect on plant development is tested. However, this approach neglects the study of their survival in soil, root-colonization, and the monitoring of beneficial functions in the rhizosphere. This could explain the recurrent lack of success in the transition from lab tests to field applications of natural isolates from novel habitats. In our recent studies, we found that native maize seeds from traditional agroecosystems carry endophytic bacterial communities that are dominated by members of the class Bacilli. As an approach to grasp their PGP potential, we developed protocols to test maize root-colonization of these natural isolates in 1) a short-term hydroponics assay in vitro and 2) a long-term assay in non-sterile soil pots. Our results show that in vitro biofilm formation was only partially associated to short-term colonization in vitro; furthermore, long-term root-colonization in soil pots was not correlated to the in vitro assays. This work highlights the necessity to incorporate root-colonization assays as part of the research strategies in the search for PGPB natural isolates from unexplored habitats, towards the generation of inoculants with increased success in the field.

microbiology↗

Irreversible temperature gating in trpv1 sheds light on channel activation

Temperature activated TRP channels or thermoTRPs are among the only proteins that can directly convert temperature changes into changes in channel open probability. In spite of a wealth of information, including several experimentally determined structural models of TRP channels, the mechanism of temperature activation remains unknown. We have carefully characterized the repeated activation of TRPV1 by thermal stimuli and discovered a previously unknown inactivation process, which is irreversible. This inactivation is associated with specific conformational changes in the membrane proximal domain. We propose that this form of gating in TRPV1 channels is a consequence of the heat absorption process that leads to channel opening.

biophysics↗