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CORRECTION article

Front. Plant Sci., 08 December 2021
Sec. Plant Pathogen Interactions
Volume 12 - 2021 | https://doi.org/10.3389/fpls.2021.812672

Corrigendum: Heat Shock Protein HSP24 Is Involved in the BABA-Induced Resistance to Fungal Pathogen in Postharvest Grapes Underlying an NPR1-Dependent Manner

This article is a correction to:

  1. Heat Shock Protein HSP24 Is Involved in the BABA-Induced Resistance to Fungal Pathogen in Postharvest Grapes Underlying an NPR1-Dependent Manner

    1. Read original article
\nChunhong Li,Chunhong Li1,2Shifeng CaoShifeng Cao3Kaituo Wang, Kaituo Wang1,2*Changyi LeiChangyi Lei1Nana JiNana Ji2Feng XuFeng Xu4Yongbo JiangYongbo Jiang1Linglan QiuLinglan Qiu1Yonghua ZhengYonghua Zheng2
  • 1College of Life and Food Engineering, Chongqing Three Gorges University, Chongqing, China
  • 2College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China
  • 3College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo, China
  • 4College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, China

A Corrigendum on
Heat Shock Protein HSP24 Is Involved in the BABA-Induced Resistance to Fungal Pathogen in Postharvest Grapes Underlying an NPR1-Dependent Manner

by Li, C., Cao, S., Wang, K., Lei, C., Ji, N., Xu, F., Jiang, Y., Qiu, L., and Zheng, Y. (2021). Front. Plant Sci. 12:646147. doi: 10.3389/fpls.2021.646147

In the original article, there was an indeterminacy in Figure 5A as published. The figure depicted a small white dot of a single colony or a little colony cluster presented on the SD-T-L-H plate. We carelessly thought the white dot to be a bubble from the process of pouring the synthetic dropout medium into Petri dishes at first, because the single colony was extremely similar to a bubble. However, the presence of an actual single colony or colony cluster in SD-T-L-H plate might be caused by the self-activation of the “bait” pGBKT7 plasmid, thus leading to the “false positive” image in Y2H experiments with a very low probability (<5%). Of course, the result of His pull-down exhibited an obvious interaction between VvHSP24 and VvNPR1 in vitro.

FIGURE 5
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Figure 5. VvHSP24 interacts with VvNPR1 in vivo and in vitro. (A) Yeast two-hybrid analysis of the physical interaction between VvHSP24 and VvNPR1. SD-T-L-H, SD/-Trp-Leu-His agar medium; SD-T-L-H-A, SD/-Trp-Leu-His-Ade agar medium. The right-angled triangles on the top of the gridded Petri dishes represent the absorbance of yeasts at 600 nm in a 10-fold dilution series, from 1 to 10−2 abs. (B) The GST-fused VvNPR1 protein (1 mL) was incubated with 1 mL of preimmobilized His-VvHSP24 protein in a total volume of 25 mL at 4°C for more than 8 h. The pulled down proteins (6 μL) were analyzed by western blotting with anti-His or anti-GST antibodies.

In past month, we re-conducted the Y2H with three replications following the method as described in the published M&M to completely confirm the interaction. Meanwhile, pull-down and co-IP were both done in this period. The obtained Y2H results showed that the colony clusters on SD-T-L-H and SD-T-L-H-A plates with or without X-α-gal were absolutely caused by the physical interaction between VvHSP24 and VvNPR1, but not the self-activation of the pGBKT7 vector, because no colony appeared among the negative controls (BD-VvHSP24 + AD and BD + AD-VvNPR1) in dropout plates. The pull-down and co-IP assays confirmed the interaction between VvHSP24 and VvNPR1 in vitro and in plant cells, which were consistent with the representative result of Y2H.

The correct Figure 5 appears below.

The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.

Publisher's Note

All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article, or claim that may be made by its manufacturer, is not guaranteed or endorsed by the publisher.

Keywords: β-aminobutyric acid, heat shock protein, priming resistance, NPR1, Botrytis cinerea, grape berries

Citation: Li C, Cao S, Wang K, Lei C, Ji N, Xu F, Jiang Y, Qiu L and Zheng Y (2021) Corrigendum: Heat Shock Protein HSP24 Is Involved in the BABA-Induced Resistance to Fungal Pathogen in Postharvest Grapes Underlying an NPR1-Dependent Manner. Front. Plant Sci. 12:812672. doi: 10.3389/fpls.2021.812672

Received: 10 November 2021; Accepted: 12 November 2021;
Published: 08 December 2021.

Edited and reviewed by: Essaid Ait Barka, Université de Reims Champagne-Ardenne, France

Copyright © 2021 Li, Cao, Wang, Lei, Ji, Xu, Jiang, Qiu and Zheng. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Kaituo Wang, wangkaituo83@gmail.com

Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.