Could Helicobacter pylori play an important role in axonal type of Guillain-Barré Syndrome pathogenesis?

Ghabaee, Mojdeh; Ghanbarian, Davod; Brujeni, Gholamreza Nikbakht; Bokaei, S; Siavoshi, Farideh; Gharibzadeh, Shahriar

doi:10.1016/j.clineuro.2009.11.008

Cited by 14 publications

(11 citation statements)

References 21 publications

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“…Indeed, epidemiological studies have shown that cardiovascular, hematological and neurological disorders are linked to infection with cagA -positive H. pylori [82,83,84,85]. Since only a small amount of CagA can be enclosed in exosomes that are then circulated to vast areas of the body, only minute amounts of CagA may be delivered to remote tissues.…”

Section: Discussionmentioning

confidence: 99%

Sequence Polymorphism and Intrinsic Structural Disorder as Related to Pathobiological Performance of the Helicobacter pylori CagA Oncoprotein

Nishikawa

Hatakeyama

2017

Toxins

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CagA, an oncogenic virulence factor produced by Helicobacter pylori, is causally associated with the development of gastrointestinal diseases such as chronic gastritis, peptic ulcers, and gastric cancer. Upon delivery into gastric epithelial cells via bacterial type IV secretion, CagA interacts with a number of host proteins through the intrinsically disordered C-terminal tail, which contains two repeatable protein-binding motifs, the Glu-Pro-Ile-Tyr-Ala (EPIYA) motif and the CagA multimerization (CM) motif. The EPIYA motif, upon phosphorylation by host kinases, binds and deregulates Src homology 2 domain-containing protein tyrosine phosphatase 2 (SHP2), a bona fide oncoprotein, inducing pro-oncogenic mitogenic signaling and abnormal cell morphology. Through the CM motif, CagA inhibits the kinase activity of polarity regulator partitioning-defective 1b (PAR1b), causing junctional and polarity defects while inducing actin cytoskeletal rearrangements. The magnitude of the pathobiological action of individual CagA has been linked to the tandem repeat polymorphisms of these two binding motifs, yet the molecular mechanisms by which they affect disease outcome remain unclear. Recent studies using quantitative techniques have provided new insights into how the sequence polymorphisms in the structurally disordered C-terminal region determine the degree of pro-oncogenic action of CagA in the gastric epithelium.

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Section: Discussionmentioning

confidence: 99%

Sequence Polymorphism and Intrinsic Structural Disorder as Related to Pathobiological Performance of the Helicobacter pylori CagA Oncoprotein

Nishikawa

Hatakeyama

2017

Toxins

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“…A rare variant of GBS, AMSAN, is generally associated with slow and incomplete recovery; interestingly, AM-SAN has been associated specifically with Helicobacter pylori infections. 1,4,7 In patients who have undergone major surgery, surgical stress may be the potential triggering factor for GBS or its variants due to predisposing infections. 6 This is the first case described of an association between AMSAN and acute colitis caused by H. pylori in the early postoperative period following surgery for a cervical chondroma.…”

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confidence: 99%

Acute motor-sensory axonal neuropathy after cervical spine surgery

Miscusi¹,

Currà

Rocca

et al. 2012

SPI

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The authors report the case of a 55-year-old man who presented with acute motor-sensory axonal neuropathy (AMSAN), a variant of Guillain-Barré syndrome with a poor prognosis, immediately after surgery for resection of a cervical chondroma. A misdiagnosis of spinal cord shock due to an acute surgical or vascular postoperative complication was initially made in this patient. Nevertheless, there was continuous transient improvement that was followed by progressive worsening, and further investigation was necessary. The diagnosis of AMSAN, associated with acute colitis caused by Helicobacter pylori, was made based on neurophysiological examinations and colonoscopy. Interestingly, the patient also developed nephrotic syndrome, which was thought to be a further complication of the autoimmune reaction. Delayed administration of immunoglobulins (400 mg/kg/day), mesalazine (800 mg 3×/day), and meropenem (3 g/day) was used to treat the Helicobacter infection and the autoimmune reaction, leading to restoration of renal function and slight neurological improvement. The patient's general condition and neurological status improved slightly, but he remained seriously disabled (Frankel Grade C). This case demonstrates that a new onset of neurological symptoms in the early postoperative period after spine surgery could be related to causes other than iatrogenic myelopathy, and that an early diagnosis can reduce neurological sequelae, leading to a better outcome.

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“…It causes diverse diseases of the stomach, from chronic gastritis to mucosa-associated lymphoid tissue lymphomas (24,25). Interestingly, recent work has shown that this organism may also have a role in autoimmune thrombocytopenia (26), Guillain-Barre syndrome (27), and in Alzheimer's disease (28) and in strokes (29). These diseases and especially ailments, such as persistent diarrhea, peptic ulcer, and gastric cancer, may be mitigated if a way can be found to eradicate H. pylori.…”

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Crystal Structure and Mode of Helicase Binding of the C-Terminal Domain of Primase from Helicobacter pylori

et al. 2013

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bTo better understand the poor conservation of the helicase binding domain of primases (DnaGs) among the eubacteria, we determined the crystal structure of the Helicobacter pylori DnaG C-terminal domain (HpDnaG-CTD) at 1.78 Å. The structure has a globular subdomain connected to a helical hairpin. Structural comparison has revealed that globular subdomains, despite the variation in number of helices, have broadly similar arrangements across the species, whereas helical hairpins show different orientations. Further, to study the helicase-primase interaction in H. pylori, a complex was modeled using the HpDnaG-CTD and HpDnaB-NTD (helicase) crystal structures using the Bacillus stearothermophilus BstDnaB-BstDnaG-CTD (helicase-primase) complex structure as a template. By using this model, a nonconserved critical residue Phe534 on helicase binding interface of DnaG-CTD was identified. Mutation guided by molecular dynamics, biophysical, and biochemical studies validated our model. We further concluded that species-specific helicase-primase interactions are influenced by electrostatic surface potentials apart from the critical hydrophobic surface residues.

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Could Helicobacter pylori play an important role in axonal type of Guillain-Barré Syndrome pathogenesis?

Cited by 14 publications

References 21 publications

Sequence Polymorphism and Intrinsic Structural Disorder as Related to Pathobiological Performance of the Helicobacter pylori CagA Oncoprotein

Sequence Polymorphism and Intrinsic Structural Disorder as Related to Pathobiological Performance of the Helicobacter pylori CagA Oncoprotein

Acute motor-sensory axonal neuropathy after cervical spine surgery

Crystal Structure and Mode of Helicase Binding of the C-Terminal Domain of Primase from Helicobacter pylori

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