Unique Cytomegalovirus Tongue Ulcer in an Older Adult Patient with Prolonged Systemic Steroid Treatment

Introduction: Cytomegalovirus (CMV) is a member of the Herpesviridae family that infects humans. It infects approximately 90% of adults. It is an opportunistic pathogen, common among immunosuppressed patients and can affect multiple organs. To date, there has been only one reported case of a CMV-related tongue ulcer that occurred during steroid treatment. Case Presentation: We report a case of CMV tongue ulcer in an elder, immunodeficient patient under prolonged steroid treatment. Management and Prognosis: A 67-year-old man under chronic steroidal treatment due to severe chronic obstructive pulmonary disease (COPD), with chronic ischemic heart disease (CIHD) and poorly treated diabetes mellitus (DM) was hospitalized in Soroka university medical center. He suffered from an ulcerative wound about 10 mm in its greater diameter with raised margins on the left lateral tongue. Daktarin Oral Gel treatment showed no improvement. On histopathological examination, a diagnosis of CMV-related tongue ulcer was given. Conclusion: To the best of our knowledge, this is the most detailed case report of CMV tongue ulcer due to prolonged steroid treatment. An early diagnosis of CMV infection in patients with oral lesions is crucial because CMV infection can increase immunosuppression, and is associated with opportunistic infections.

Metal ion binding to concanavalin A.

Metal ion activation of saccharide binding has been studied for concanavalin A near pH 7.0. Although two metal ions, a transition metal ion and a Ca2+ ion, can bind, both are not required. Ca2+ alone, Mn2+ alone, or Ca2+ with other transition metal ions can activate this lectin. Only one Ca2+ ion per subunit or only one Mn2+ per subunit is sufficient. Metal ion binding was studied by magnetic resonance techniques and direct binding assays. Saccharide binding activity was monitored by following the fluorescence of 4-methylumbelliferyl a-D-mannopyranoside. When Ca2+ binds to demetalized concanavalin A, the transition metal ion site is hindered. When Mn2+ alone binds to demetalized concanavalin A, saccharide binding activity is induced. A subsequent conformational change, not necessary for carbohydrate binding activity, covers the Mn2+.