PMID- 34082810
OWN - NLM
STAT- MEDLINE
DCOM- 20210927
LR  - 20210927
IS  - 1297-9716 (Electronic)
IS  - 0928-4249 (Print)
IS  - 0928-4249 (Linking)
VI  - 52
IP  - 1
DP  - 2021 Jun 3
TI  - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) moonlights as an adhesin in 
      Mycoplasma hyorhinis adhesion to epithelial cells as well as a plasminogen 
      receptor mediating extracellular matrix degradation.
PG  - 80
LID - 10.1186/s13567-021-00952-8 [doi]
LID - 80
AB  - Mycoplasma hyorhinis infects pigs causing polyserositis and polyarthritis, and 
      has also been reported in a variety of human tumor tissues. The occurrence of 
      disease is often linked with the systemic invasion of the pathogen. 
      Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH), one of the key enzymes of 
      glycolysis, was reported as a surface multifunctional molecule in several 
      bacteria. Here, we investigated whether GAPDH could manifest binary functions; as 
      an adhesin to promote colonization as well as a plasminogen receptor functioning 
      in extracellular matrix (ECM) degradation to promote systemic invasion. The 
      surface localization of GAPDH was observed in M. hyorhinis with flow cytometry 
      and colony blot analysis. Recombinant GAPDH (rGAPDH) was found to be able to bind 
      porcine-derived PK-15 and human-derived NCI-H292 cells. The incubation with 
      anti-GAPDH antibody significantly decreased the adherence of M. hyorhinis to both 
      cell lines. To investigate its function in recruiting plasminogen, firstly, the 
      interaction between rGAPDH and plasminogen was demonstrated by ELISA and 
      Far-Western blot assay. The activation of the rGAPDH-bound plasminogen into 
      plasmin was proved by using a chromogenic substrate, and furtherly confirmed to 
      degrade extracellular matrix by using a reconstituted ECM. Finally, the ability 
      of rGAPDH to bind different ECM components was demonstrated, including 
      fibronectin, laminin, collagen type IV and vitronectin. Collectively, our data 
      imply GAPDH as an important adhesion factor of M. hyrohinis and a receptor for 
      hijacking host plasminogen to degrade ECM. The multifunction of GAPDH to bind 
      both plasminogen and ECM components is believed to increase the targeting of 
      proteolysis and facilitate the dissemination of M. hyorhinis.
FAU - Wang, Jia
AU  - Wang J
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa.
FAU - Li, Yao
AU  - Li Y
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
AD  - School of Life Sciences, Jiangsu University, Zhenjiang, China.
FAU - Pan, Longji
AU  - Pan L
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Li, Jun
AU  - Li J
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Yu, Yanfei
AU  - Yu Y
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
AD  - College of Veterinary Medicine, Hunan Agricultural University, Changsha, China.
AD  - School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
FAU - Liu, Beibei
AU  - Liu B
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Zubair, Muhammad
AU  - Zubair M
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Wei, Yanna
AU  - Wei Y
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Pillay, Bala
AU  - Pillay B
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa.
FAU - Olaniran, Ademola Olufolahan
AU  - Olaniran AO
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa.
FAU - Chiliza, Thamsanqa E
AU  - Chiliza TE
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa.
FAU - Shao, Guoqing
AU  - Shao G
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa.
AD  - School of Food and Biological Engineering, Jiangsu University, Zhenjiang, China.
FAU - Feng, Zhixin
AU  - Feng Z
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China.
FAU - Xiong, Qiyan
AU  - Xiong Q
AUID- ORCID: 0000-0002-2922-9875
AD  - Institute of Veterinary Medicine, Key Laboratory of Veterinary Biological 
      Engineering and Technology, Ministry of Agriculture, Jiangsu Academy of 
      Agricultural Sciences, Nanjing, China. qiyanxiongnj@163.com.
AD  - College of Agriculture, Engineering & Science, University of KwaZulu-Natal, 
      Durban, South Africa. qiyanxiongnj@163.com.
AD  - School of Life Sciences, Jiangsu University, Zhenjiang, China. 
      qiyanxiongnj@163.com.
LA  - eng
GR  - 31770193/National Natural Science Foundation of China/
GR  - 31700158/National Natural Science Foundation of China/
GR  - BRA2020370/333 High-level Personnel Training Project of Jiangsu Province of 
      China/
GR  - NY-015/Six Talent Peaks Project in Jiangsu Province/
GR  - CX(20)3090/Jiangsu Agricultural Science and Technology Independent Innovation 
      Fund/
GR  - BK20190261/Natural Science Foundation of Jiangsu Province/
PT  - Journal Article
DEP - 20210603
PL  - England
TA  - Vet Res
JT  - Veterinary research
JID - 9309551
RN  - 0 (Adhesins, Bacterial)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 9001-91-6 (Plasminogen)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
SB  - IM
MH  - Adhesins, Bacterial/*genetics/metabolism
MH  - Animals
MH  - Bacterial Adhesion/physiology
MH  - Bacterial Proteins/*genetics/metabolism
MH  - Cell Line
MH  - Epithelial Cells/microbiology/physiology
MH  - Extracellular Matrix
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/*genetics/metabolism
MH  - Humans
MH  - Mycoplasma hyorhinis/genetics/*physiology
MH  - Plasminogen/metabolism
MH  - Receptors, Cell Surface/*genetics/metabolism
MH  - Sus scrofa
PMC - PMC8173509
OTO - NOTNLM
OT  - Adhesion
OT  - Extracellular matrix
OT  - GAPDH
OT  - M. hyorhinis
OT  - Plasminogen
COIS- The authors declare that they have no competing interests.
EDAT- 2021/06/05 06:00
MHDA- 2021/09/28 06:00
PMCR- 2021/06/03
CRDT- 2021/06/04 05:41
PHST- 2021/03/09 00:00 [received]
PHST- 2021/05/11 00:00 [accepted]
PHST- 2021/06/04 05:41 [entrez]
PHST- 2021/06/05 06:00 [pubmed]
PHST- 2021/09/28 06:00 [medline]
PHST- 2021/06/03 00:00 [pmc-release]
AID - 10.1186/s13567-021-00952-8 [pii]
AID - 952 [pii]
AID - 10.1186/s13567-021-00952-8 [doi]
PST - epublish
SO  - Vet Res. 2021 Jun 3;52(1):80. doi: 10.1186/s13567-021-00952-8.