Etiologies of benign esophageal dysphagia are diverse and a panel of clinical and laboratory investigations should be taken to make the right diagnosis. We report herein two cases of benign esophageal dysphagia of non...Etiologies of benign esophageal dysphagia are diverse and a panel of clinical and laboratory investigations should be taken to make the right diagnosis. We report herein two cases of benign esophageal dysphagia of non-infectious origin. Imaging tests identified changes similar to malignancies, while only inflamed granulation tissue was discovered in biopsy specimens. Surgical resection was finally applied due to severe symptoms and the histological study revealed only granulation tissue. They were diagnosed as idiopathic cases when all the known non-infectious pathogenesis were carefully ruled out by sound examination results. The differetail diagnosis of benign esophageal dysphagia is quite important as observational data shows that medical therapy should be applied in certain pathogenesis, while esophagectomy might be the most effective solution for other etiologies. Subsequently a comparison of the manifestations of the two cases and those of esophageal dysphagia induced by other non-infectious etiologies was done to shine some light on the differencial diagnosis of benign esophageal dysphagia.展开更多
The henipaviruses,represented by Nipah virus and Hendra virus,are emerging zoonotic viral pathogens responsible for repeated outbreaks associated with high morbidity and mortality in Australia,Southeast Asia,India and...The henipaviruses,represented by Nipah virus and Hendra virus,are emerging zoonotic viral pathogens responsible for repeated outbreaks associated with high morbidity and mortality in Australia,Southeast Asia,India and Bangladesh. These viruses enter host cells via a class I viral fusion mechanism mediated by their attachment and fusion envelope glycoproteins;efficient membrane fusion requires both these glycoproteins in conjunction with specific virus receptors present on susceptible host cells. The henipavirus attachment glycoprotein interacts with a cellular B class ephrin protein receptor triggering conformational alterations leading to the activation of the viral fusion(F) glycoprotein. The analysis of monoclonal antibody(mAb) reactivity with G has revealed measurable alterations in the antigenic structure of the glycoprotein following its binding interaction with receptor. These observations only appear to occur with full-length native G glycoprotein,which is a tetrameric oligomer,and not with soluble forms of G(sG) ,which are disulfide-linked dimers. Single amino acid mutations in a heptad repeat-like structure within the stalk domain of G can disrupt its association with F and subsequent membrane fusion promotion activity. Notably,these mutants of G also appear to confer a post-receptor bound conformation implicating the stalk domain as an important element in the G glycoprotein's structure and functional relationship with F. Together,these observations suggest fusion is dependent on a specific interaction between the F and G glycoproteins of the henipaviruses. Further,receptor binding induces measurable changes in the G glycoprotein that appear to be greatest in respect to the interactions between the pairs of dimers comprising its native tetrameric structure. These receptor-induced conformational changes may be associated with the G glycoprotein's promotion of the fusion activity of F.展开更多
基金Supported by Scientific and Technological Project of Shaanxi Province (2011K12-05-10)
文摘Etiologies of benign esophageal dysphagia are diverse and a panel of clinical and laboratory investigations should be taken to make the right diagnosis. We report herein two cases of benign esophageal dysphagia of non-infectious origin. Imaging tests identified changes similar to malignancies, while only inflamed granulation tissue was discovered in biopsy specimens. Surgical resection was finally applied due to severe symptoms and the histological study revealed only granulation tissue. They were diagnosed as idiopathic cases when all the known non-infectious pathogenesis were carefully ruled out by sound examination results. The differetail diagnosis of benign esophageal dysphagia is quite important as observational data shows that medical therapy should be applied in certain pathogenesis, while esophagectomy might be the most effective solution for other etiologies. Subsequently a comparison of the manifestations of the two cases and those of esophageal dysphagia induced by other non-infectious etiologies was done to shine some light on the differencial diagnosis of benign esophageal dysphagia.
基金supported in part by NIH grant AI054715 to C.C.B.
文摘The henipaviruses,represented by Nipah virus and Hendra virus,are emerging zoonotic viral pathogens responsible for repeated outbreaks associated with high morbidity and mortality in Australia,Southeast Asia,India and Bangladesh. These viruses enter host cells via a class I viral fusion mechanism mediated by their attachment and fusion envelope glycoproteins;efficient membrane fusion requires both these glycoproteins in conjunction with specific virus receptors present on susceptible host cells. The henipavirus attachment glycoprotein interacts with a cellular B class ephrin protein receptor triggering conformational alterations leading to the activation of the viral fusion(F) glycoprotein. The analysis of monoclonal antibody(mAb) reactivity with G has revealed measurable alterations in the antigenic structure of the glycoprotein following its binding interaction with receptor. These observations only appear to occur with full-length native G glycoprotein,which is a tetrameric oligomer,and not with soluble forms of G(sG) ,which are disulfide-linked dimers. Single amino acid mutations in a heptad repeat-like structure within the stalk domain of G can disrupt its association with F and subsequent membrane fusion promotion activity. Notably,these mutants of G also appear to confer a post-receptor bound conformation implicating the stalk domain as an important element in the G glycoprotein's structure and functional relationship with F. Together,these observations suggest fusion is dependent on a specific interaction between the F and G glycoproteins of the henipaviruses. Further,receptor binding induces measurable changes in the G glycoprotein that appear to be greatest in respect to the interactions between the pairs of dimers comprising its native tetrameric structure. These receptor-induced conformational changes may be associated with the G glycoprotein's promotion of the fusion activity of F.
