Pancreatitis in hand-foot-and-mouth disease caused by enterovirus 71

Zhang, Yufeng; Deng, Huiling; Fu, Jia; Jian-qiang, Wei

doi:10.3748/wjg.v22.i6.2149

Cited by 15 publications

(7 citation statements)

References 15 publications

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“…Coxsackievirus group A infection usually has mild symptoms and a good prognosis. Enteroviruses, such as coxsackievirus group B and enterovirus 71, are reported to be common causes of acute pancreatitis 2 3 4 5) . In China, a 2-year-old girl was admitted because of acute abdominal pain and vomiting for 2 days and diagnosed with acute pancreatitis.…”

Section: Discussionmentioning

confidence: 99%

Acute pancreatitis in hand, foot and mouth disease caused by Coxsackievirus A16: case report

et al. 2017

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Coxsackievirus A16 (CA16), which primarily causes hand, foot, and mouth disease (HFMD), is associated with complications, such as encephalitis, acute flaccid paralysis, myocarditis, pericarditis, and shock. However, no case of pancreatitis associated with CA16 has been reported in children. We report a case of CA16-associated acute pancreatitis in a 3-year-old girl with HFMD. She was admitted because of poor oral intake and high fever for 1 day. Maculopapular rashes on both hands and feet and multiple vesicles on the soft palate were observed on physical examination. She was treated conservatively with intravenous fluids. On the fourth hospital day, she had severe abdominal pain and vomiting. The serum levels of amylase and lipase were remarkably elevated (amylase, 1,902 IU/L; reference range, 28–100 IU/L; lipase, >1,500 IU/L; reference range, 13–60 IU/L), and ultrasonography showed diffuse swelling of the pancreas with a small amount of ascites. The real-time reverse transcription polymerase chain reaction result from a stool sample was positive for CA16. CA16 can cause acute pancreatitis, and should be considered in the differential diagnosis of abdominal pain in children with HFMD.

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Section: Discussionmentioning

confidence: 99%

Acute pancreatitis in hand, foot and mouth disease caused by Coxsackievirus A16: case report

et al. 2017

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“…It is an inflammatory condition leading to morphological changes in the pancreas, causing pain and functional abnormalities. Alcohol (Pandol et al, 2010), malnutrition (Witt & Bhatia, 2008), gallstones (Levy et al, 2014), familial clustering (Kereszturi et al, 2009) and sometimes severe infections (Zhang et al, 2016) have been observed to be significant causes of pancreatitis. Pancreatitis is broadly classified (Sarner & Cotton, 1984) as acute and chronic.…”

Section: Introductionmentioning

confidence: 99%

Structural, functional and molecular dynamics analysis of cathepsin B gene SNPs associated with tropical calcific pancreatitis, a rare disease of tropics

Singh

Magani

Sharma

et al. 2019

PeerJ

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Tropical Calcific Pancreatitis (TCP) is a neglected juvenile form of chronic non-alcoholic pancreatitis. Cathepsin B (CTSB), a lysosomal protease involved in the cellular degradation process, has recently been studied as a potential candidate gene in the pathogenesis of TCP. According to the Cathepsin B hypothesis, mutated CTSB can lead to premature intracellular activation of trypsinogen, a key regulatory mechanism in pancreatitis. So far, CTSB mutations have been studied in pancreatitis and neurodegenerative disorders, but little is known about the structural and functional effect of variants in CTSB. In this study, we investigated the effect of single nucleotide variants (SNVs) specifically associated with TCP, using molecular dynamics and simulation algorithms. There were two non-synonymous variants (L26V and S53G) of CTSB, located in the propeptide region. We tried to predict the effect of these variants on structure and function using multiple algorithms: SIFT, Polyphen2, PANTHER, SDM sever, i-Mutant2.0 suite, mCSM algorithm, and Vadar. Further, using databases like miRdbSNP, PolymiRTS, and miRNASNP, two SNPs in the 3′UTR region were predicted to affect the miRNA binding sites. Structural mutated models of nsSNP mutants (L26V and S53G) were prepared by MODELLER v9.15 and evaluated using TM-Align, Verify 3D, ProSA and Ramachandran plot. The 3D mutated structures were simulated using GROMACS 5.0 to predict the impact of these SNPs on protein stability. The results from in silico analysis and molecular dynamics simulations suggested that these variants in the propeptide region of Cathepsin B could lead to structural and functional changes in the protein and thus could be pathogenic. Hence, the structural and functional analysis results have given interim conclusions that these variants can have a deleterious effect in TCP pathogenesis, either uniquely or in combination with other mutations. Thus, it could be extrapolated that Cathepsin B gene can be screened in samples from all TCP patients in future, to decipher the distribution of variants in patients.

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“…It is an inflammatory condition leading to morphological changes in the pancreas, causing pain and functional abnormalities. Alcohol(1), malnutrition (2), gallstones(3), familial clustering (4) and sometimes severe infections (5) have been observed to be significant causes of pancreatitis.…”

Section: Introductionmentioning

confidence: 99%

Peer Review #1 of "Structural, functional and molecular dynamics analysis of cathepsin B gene SNPs associated with tropical calcific pancreatitis, a rare disease of tropics (v0.1)"

2019

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Tropical Calcific Pancreatitis (TCP) is a neglected juvenile form of chronic non-alcoholic pancreatitis. Cathepsin B (CTSB), a lysosomal protease involved in the cellular degradation process, has recently been studied as a potential candidate gene in the pathogenesis of TCP. According to Cathepsin B hypothesis, mutated CTSB can lead to premature intracellular activation of trypsinogen, a key regulatory mechanism in pancreatitis. So far, CTSB mutations have been studied in pancreatitis and neurodegenerative disorders, but little is known about the structural and functional effect of variants in CTSB. In this study, we investigated the effect of single nucleotide variants (SNVs) specifically associated with TCP, using molecular dynamics and simulation algorithms. There were two nonsynonymous variants (L26V and S53G) of CTSB, located in the propeptide region. We tried to predict the effect of these variants on structure and function using multiple algorithms: SIFT, Polyphen2, PANTHER, SDM sever, i-Mutant2.0 suite, mCSM algorithm, and Vadar. Further, using databases like miRdbSNP, PolymiRTS, and miRNASNP, two SNPs in the 3'UTR region were predicted to affect the miRNA binding sites. Structural mutated models of nsSNP mutants (L26V and S53G) were prepared by MODELLER v9.15 and evaluated using TM-Align, Verify 3D, ProSA and Ramachandran plot. The 3D mutated structures were simulated using GROMACS 5.0 to predict the impact of these SNPs on protein stability. The results from in silico analysis and molecular dynamics simulations suggested that these variants in the propeptide region of Cathepsin B could lead to structural and functional changes in the protein and thus could be pathogenic. Hence, the structural and functional analysis results have given interim conclusions that these variants can have a deleterious effect in TCP pathogenesis, either uniquely or in combination with other mutations. Thus, it could be extrapolated that Cathepsin B gene can be screened in samples from all TCP patients in future, to decipher the distribution of variants in patients.

show abstract

Pancreatitis in hand-foot-and-mouth disease caused by enterovirus 71

Cited by 15 publications

References 15 publications

Acute pancreatitis in hand, foot and mouth disease caused by Coxsackievirus A16: case report

Acute pancreatitis in hand, foot and mouth disease caused by Coxsackievirus A16: case report

Structural, functional and molecular dynamics analysis of cathepsin B gene SNPs associated with tropical calcific pancreatitis, a rare disease of tropics

Peer Review #1 of "Structural, functional and molecular dynamics analysis of cathepsin B gene SNPs associated with tropical calcific pancreatitis, a rare disease of tropics (v0.1)"

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