TY - JOUR
T1 - Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131
T2 - a proteomics approach using mass spectrometry
AU - Nakamura, Akihiro
AU - Komatsu, Masaru
AU - Ohno, Yuki
AU - Noguchi, Nobuyoshi
AU - Kondo, Akira
AU - Hatano, Naoya
N1 - Funding Information:
We are grateful to the members of the Association of Japan Community Healthcare Organization (JCHO) hospitals and the Study of Bacterial Resistance in the Kinki Region of Japan (SBRK) Medical Technologists for their help during the collection of the strains. This work was supported by JSPS KAKENHI (grant number 18K16189) and internal funding.
Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteristics. Five proteins had ST131-specific amino acid substitutions: uncharacterized protein YahO with E34A (m/z 7655); UPF0337 protein YjbJ with V59D, D60S and T63K (m/z 8351); uncharacterized protein YnfD with S106T (m/z 8448); and acid stress chaperone HdeA with Q92K and N94S (m/z 9714). Soluble cytochrome b562 (m/z 11783) showed seven amino acid substitutions, and the sequence differed between clade C of the pandemic clade and non-C. In silico analysis showed YahO protein-protein interaction with YjbJ, possibly related to biofilm formation. Although the function of soluble cytochrome b562 is electron transport of unknown function, its involvement in biofilm formation was predicted. HdeA was a gastric acid resistance-related protein. The function of YnfD was completely unclear. In conclusion, ST131-specific protein amino acid substitutions consisted mainly of a gastric acid resistance protein and proteins of unknown function (possibly involved in biofilm formation), which might be mechanisms for long-term colonization in the human intestinal tract.
AB - The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteristics. Five proteins had ST131-specific amino acid substitutions: uncharacterized protein YahO with E34A (m/z 7655); UPF0337 protein YjbJ with V59D, D60S and T63K (m/z 8351); uncharacterized protein YnfD with S106T (m/z 8448); and acid stress chaperone HdeA with Q92K and N94S (m/z 9714). Soluble cytochrome b562 (m/z 11783) showed seven amino acid substitutions, and the sequence differed between clade C of the pandemic clade and non-C. In silico analysis showed YahO protein-protein interaction with YjbJ, possibly related to biofilm formation. Although the function of soluble cytochrome b562 is electron transport of unknown function, its involvement in biofilm formation was predicted. HdeA was a gastric acid resistance-related protein. The function of YnfD was completely unclear. In conclusion, ST131-specific protein amino acid substitutions consisted mainly of a gastric acid resistance protein and proteins of unknown function (possibly involved in biofilm formation), which might be mechanisms for long-term colonization in the human intestinal tract.
UR - http://www.scopus.com/inward/record.url?scp=85067304240&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85067304240&partnerID=8YFLogxK
U2 - 10.1038/s41598-019-45051-z
DO - 10.1038/s41598-019-45051-z
M3 - Article
C2 - 31189981
AN - SCOPUS:85067304240
SN - 2045-2322
VL - 9
JO - Scientific Reports
JF - Scientific Reports
IS - 1
M1 - 8555
ER -