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Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation

The Endosomal Sorting Complex Required for Transport-III (ESCRT-III) is part of a conserved membrane remodeling machine. ESCRT-III employs polymer formation to catalyze inside-out membrane fission processes in a large variety of cellular processes, including budding of endosomal vesicles and enveloped viruses, cytokinesis, nuclear envelope reformation, plasma membrane repair, exosome formation, neuron pruning, dendritic spine maintenance, and preperoxisomal vesicle biogenesis.*

How membrane shape influences ESCRT-III polymerization and how ESCRT-III shapes membranes is yet unclear.*

In the article “Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation” Aurélie Bertin, Nicola de Franceschi, Eugenio de la Mora, Sourav Maity, Maryam Alqabandi, Nolwen Miguet, Aurélie di Cicco, Wouter H. Roos, Stéphanie Mangenot, Winfried Weissenhorn and Patricia Bassereau describe how human core ESCRT-III proteins, CHMP4B, CHMP2A, CHMP2B and CHMP3 are used to address this issue in vitro by combining membrane nanotube pulling experiments, cryo-electron tomography and Atomic Force Microscopy.*

The authors show that CHMP4B filaments preferentially bind to flat membranes or to tubes with positive mean curvature.*

The results presented in the article cited above underline the versatile membrane remodeling activity of ESCRT-III that may be a general feature required for cellular membrane remodeling processes.*

The authors provide novel insight on how mechanics and geometry of the membrane and of ESCRT-III assemblies can generate forces to shape a membrane neck.*

NanoWorld Ultra-Short AFM Cantilevers USC-F1.2-k0.15 were used for the High-speed Atomic Force Microscopy ( HS-AFM ) experiments presented in this article.*

Figure 1 from «Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation” by Aurélie Bertin et al.:
CHMP4-ΔC flattens LUVs and binds preferentially to flat membranes or to membranes with a positive mean curvature.
1a CHMP4B-ΔC spirals observed by HS-AFM on a lipid bilayer. Scale bar: 50 nm.
Please refer to the full article for the complete figure: https://rdcu.be/b5rOe — Figure 1 from «*Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation*” by Aurélie Bertin et al.:
CHMP4-ΔC flattens LUVs and binds preferentially to flat membranes or to membranes with a positive mean curvature.
1a CHMP4B-ΔC spirals observed by HS-AFM on a lipid bilayer. Scale bar: 50 nm.
Please refer to the full article for the complete figure: https://rdcu.be/b5rOe

*Aurélie Bertin, Nicola de Franceschi, Eugenio de la Mora, Sourav Maity, Maryam Alqabandi, Nolwen Miguet, Aurélie di Cicco, Wouter H. Roos, Stéphanie Mangenot, Winfried Weissenhorn and Patricia Bassereau
Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation
Nature Communications volume 11, Article number: 2663 (2020)
DOI: https://doi.org/10.1038/s41467-020-16368-5

Please follow this external link to read the full article: https://rdcu.be/b5rO e

Open Access The article “ Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation “ by Aurélie Bertin, Nicola de Franceschi, Eugenio de la Mora, Sourav Maity, Maryam Alqabandi, Nolwen Miguet, Aurélie di Cicco, Wouter H. Roos, Stéphanie Mangenot, Winfried Weissenhorn and Patricia Bassereau is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

Pectin Interaction with Immune Receptors is Modulated by Ripening Process in Papayas

Dietary fibers have been shown to exert immune effects via interaction with pattern recognition receptors (PRR) such as toll-like receptors (TLR) and nucleotide-binding oligomerization domain (NOD)-like receptors. Pectin is a dietary fiber that interacts with PRR depending on its chemical structure. Papaya pectin retains different chemical structures at different ripening stages. How this influences PRR signalling is unknown.*

The aim of the article “Pectin Interaction with Immune Receptors is Modulated by Ripening Process in Papayas” by Samira B. R. Prado, Martin Beukema, Eva Jermendi, Henk A. Schols, Paul de Vos and João Paulo Fabi was to determine how ripening influences pectin structures and their ability to interact with TLR2, 3, 4, 5 and 9, and NOD1 and 2.*

Papaya ripening is an enzymatic, biochemically driven process that occurs over a short period of time (five days) and involves the mobilization of pectin and the alteration of its chemical composition.

The authors evaluated the interaction of the water-soluble fractions rich in pectin extracted from unripe to ripe papayas. The pectin extracted from ripe papayas activated all the TLR and, to a lesser extent, the NOD receptors. The pectin extracted from unripe papayas also activated TLR2, 4 and 5 but inhibited the activation of TLR3 and 9.*

During papaya ripening, profound changes in pectin structures lead to differences in the biological effects. The data presented in the paper show that papaya pectin extracted from fruit pulp at different ripening points differently interacted with PRR in a ripening-dependent way. The longer chains of HG from unripe papayas pectin, which were less methyl-esterified, inhibited the activation of TLR3 and 9 and activated TLR2 and 4, in contrast to the ripe papaya’s pectin, which have smaller HG chains with medium methyl esterification thus activating TLR2, 3, 4, 5 and 9.*

This variation may represent new biological features of papaya pectin structures in addition to anticancer activities, possibly creating new and cost-effective approaches to extracting papaya pectin with desirable structural and biological features.*

These findings might lead to selection of ripening stages for tailored modulation of PRR to support or attenuate immunity in consumers.*

The changes in Molecular weight ( Mw ) can also be visualized by Atomic Force Microscopy (see Fig. 1C in the paper.)

The AFM images presented in the paper were acquired in tapping mode using an NanoWorld Pointprobe® NCHR AFM probe with a typical spring constant of 42 N/m and typically 320 kHz resonance frequency. The scan speed and scanning resolution were 0.5 Hz and 512 × 512 points, respectively.*

Figure 1 C from “Pectin Interaction with Immune Receptors is Modulated by Ripening Process in Papayas” by Samira B. R. Prado et al. 2020:
(C) Representative topographical AFM images of Un-1-WSF and R-2-WSF. White arrow indicates linear structures, black arrow aggregates and grey arrow the smaller structure from the R-2-WSF. Un-1-WSF: unripe – papaya from 1st day after harvest – water-soluble fraction; Un-2-WSF: unripe – papaya from 2nd day after harvest – water-soluble fraction; I-WSF: intermediate ripening time point – papaya from 3rd day after harvest – water-soluble fraction; R-1-WSF: ripe – papaya from 4th day after harvest – water-soluble fraction; R-2-WSF: ripe – papaya from 5th day after harvest – water-soluble fraction. Please have a look at the full article for the full figure.

*Samira B. R. Prado, Martin Beukema, Eva Jermendi, Henk A. Schols, Paul de Vos and João Paulo Fabi
Pectin Interaction with Immune Receptors is Modulated by Ripening Process in Papayas
Nature Scientific Reports volume 10, Article number: 1690 (2020)
DOI: https://doi.org/10.1038/s41598-020-58311-0

Please follow this external link to read the full article htt ps://rdcu.be/b3Fnb .

Open Access The article “ Pectin Interaction with Immune Receptors is Modulated by Ripening Process in Papayas “ by Samira B. R. Prado, Martin Beukema, Eva Jermendi, Henk A. Schols, Paul de Vos and João Paulo Fabi is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

We’re at the Biophysical Society Meeting in San Diego this week

We’re at NanoAndMore USA booth no. 818 at the Biophysical Society Meeting in San Diego this week. Have you already visited us and found out what’s up with the giant AFM probe at the booth?