Corrigendum

In Deb et al. (2019), published in Mol. Plant Pathol. 20, 976‐989, the authors noticed some errors in the main Article and Supporting Information which are due to improper labels in some of the figures, figure legends and table.

The corrections are listed as follows:

Page 978: In Figure 1 caption, “cVFP::xopQ, nVFP::Gf14f and nVFP::Gf14g” should be written instead of “nVFP::xopQ, cVFP::Gf14f and cVFP::Gf14g”. The figure caption should read as follows:

Fig. 1 The X. oryzae pv. oryzae XopQ protein interacts with two rice 14‐3‐3 proteins, Gf14f and Gf14g. (A) Yeast strain pJ694a containing bait vector BD::XopQ was independently transformed with the following prey constructs: AD::Gf14a‐h. Transformed colonies were serially diluted and spotted on the non‐selective (SD‐LT; double dropout, DDO) and selective (SD‐ALTH; quadruple dropout, QDO) media with 1 mM 3‐amino‐1,2,4‐triazole. Observations were noted after 3 days of incubation at 30 °C. (B) For BiFC analysis of XopQ–14‐3‐3 interactions, leaves of N. benthamiana were hand‐infiltrated with a suspension (8 × 10⁸ CFU/mL) of two A. tumefaciens AGL1 strains containing empty vectors alone or cVFP::XopQ and nVFP::Gf14f or nVFP::Gf14g. Fluorescence was visualized in a confocal microscope (Carl Zeiss LSM880, Oberkochen, Germany) at 20 × magnification and excitation wavelength (488 nm) 48 h after infiltration. Bar, 50 μm. The experiment was repeated three times with similar results.

Page 979: In Fig 2B, the figure labels had been positioned such that the entire label is not visible. It has been corrected in the revised image below. Also, in Figure 2 caption, the following text should read as “cVFP::xopQ, cVFP::xopQ S65A or cVFP::xopQ S65D and nVFP::Gf14f or nVFP::Gf14g” instead of “nVFP::xopQ, nVFP::xopQ S65A or nVFP::xopQ S65D and cVFP::Gf14f or cVFP::Gf14g” and “eVFP” should read as “cVFP”. The revised Figure 2 and its caption are as follows:

Fig. 2 The serine‐65 containing motif‐1 14‐3‐3 protein binding motif of XopQ is essential for its interaction with the 14‐3‐3 proteins Gf14f and Gf14g. (A) Yeast two‐hybrid analysis. The yeast strain pJ694a carrying the bait vector pDEST32 containing xopQ, xopQ S65A or xopQ S65D was independently transformed with the following prey constructs: pDEST22 containing Gf14f or Gf14g. Transformed colonies were spotted on non‐selective (SD‐LT) and selective (SD‐ALTH) media with 1 mM 3‐amino‐1,2,4‐triazole and then incubated at 30 °C for 3 days. (B, C) BiFC analysis of XopQ–14‐3‐3 interactions in N. benthamiana. Leaves were hand‐infiltrated with a suspension (8 × 10⁸ CFU/mL total) of two A. tumefaciens strains containing cVFP::xopQ, cVFP::xopQS65A or cVFP::xopQS65D and nVFP::Gf14f or nVFP::Gf14g. Fluorescence was visualized in a confocal microscope (Zeiss LSM880) at 20 × magnification and excitation wavelength (488 nm) 48 h after infiltration. Bar, 50 μm. Similar results were obtained in three independent experiments.

Pages 980 and 981: Fig 3C has been erroneously written as Fig 3B in the legend and text. The “Fig. 3B” which cited on page 980 should read as “Fig. 3C” and “Fig. 3A” should read as “Fig. 3A, B”. The Figure 3 caption should also read as follows:

Fig. 3 The serine‐65 containing 14‐3‐3 protein binding motif of XopQ is essential for suppression of rice immune responses. (A, B) For callose deposition assay, leaves of 2‐week‐old rice seedlings were infiltrated with one of the following: MilliQ water (MQ), X. oryzae pv. oryzae BXO43 (WT), xopN xopQ xopX xopZ QM, and QM harbouring the following plasmids: pHM1, pHM1::xopQ, pHM1::xopQS65A, pHM1::xopQS65D and pHM1::xopQT222A. The leaves were stained 16 h later with aniline blue and visualized under an epifluorescence microscope (365 nm). Mean and standard deviation were calculated for the number of callose deposits observed per leaf. Error bars indicate the standard deviation of readings from five infiltrated leaves. Columns in plots capped with the same letter were not significantly different from each other based on analysis of variance done using the Tukey–Kramer honestly significance difference test (P < 0.05). Bar, 100 μm. The experiment was repeated three times and similar results were obtained. (C) Rice roots were treated with one of the following: water, xopN xopQ xopX xopZ QM containing the following constructs: pHM1, pHM1::xopQ, pHM1::xopQS65A, pHM1::xopQS65D or pHM1::xopQT222A. Treated roots were subsequently stained with PI and observed under a confocal microscope using 63 × oil immersion objectives and an He‐Ne laser at 543 nm excitation to detect PI internalization. Five roots were imaged for each construct per experiment. Bar, 20 μm. Internalization of PI is indicative of defence response‐associated programmed cell death. Similar results were obtained in three independent experiments.

Page 983: The graphs in Figure 5B and 5D had been interchanged. The correct figure is as shown below:

Page 985: In Figure 6B, the labels erroneously mention “Gf14e” as “Gf1e”. The correct figure is as shown below:

Page 989: In Figure S2 caption, “xopQ‐” should read as “XopQ‐”. The correct figure caption should read as follows:

Fig. S2 Expression of xopQ gene of Xanthomonas oryzae pv. oryzae and its 14‐3‐3 protein‐binding motif mutants from exudate of rice leaves following X. oryzae pv. oryzae infection. Leaves of 40‐day‐old rice seedlings of Taichung Native 1 rice variety were clip inoculated with the following X. oryzae pv. oryzae strains: XopQ‐,XopQ‐ /pHM1, XopQ‐/pHM1::XopQ, XopQ‐/pHM1::XopQ S65A, XopQ‐/pHM1::XopQ S65D and XopQ‐/pHM1::XopQ T222A. Twelve days after inoculation, 3 cm leaf pieces from the inoculated end were cut and exudate was allowed to ooze out for 6 h at 4 °C. Expression of XopQWT and mutant proteins was detected by western blot analysis using anti:XopQ antibodies raised in rabbit. For immunoblotting using alkaline phosphatase (ALP), ALP conjugated to anti‐rabbit immunoglobulin G (Sigma, St. Louis, Missouri, USA; A3687 1ML) secondary antibody was used. XopQ expression was detected at 50 kDa (upper panel). Expression of the type II secretion system secreted enzyme lipase A was assessed by western blotting to normalize for protein loading by using anti‐lipase A antibody raised in rabbit (lower panel) and ALP based secondary antibody.

Lastly, the new version of Table S1 has been resupplied to correct the reference of Sinha et al., 2014 to Sinha et al., 2013.

The published version of the article has been corrected online.

The authors apologize for any inconvenience it may have caused.