TY - JOUR
T1 - A neutralizing monoclonal antibody against Coxsackievirus B4 cross-reacts with contractile muscle proteins
AU - Beisel, Kirk W.
AU - Srinivasappa, Javaraiah
AU - Olsen, Margaret R.
AU - Stiff, Anne C.
AU - Essani, Karim
AU - Prabhakar, Bellur S.
N1 - Funding Information:
Purification of CB4. The prototype JVB strain of CVB4 was grown and purified as previously described ." The purified virus was subjected to SDS-PAGE 14 and Western blot analysis-15 This work was supported in part by U .S Public Health Service grant HL-38276 from the National Heart, Lung and Blood Institute . The authors acknowledge Dr Abner Louis Notkins for his support and critical review of the manuscript, the technical assistance of Patricia Pepler, Laura Poole and Sara Sells in preparation of the various murine cardiac and skeletal muscle tissue and Karen Hardman and Eloise Mange for their skill in preparing the manuscript .
PY - 1990/2
Y1 - 1990/2
N2 - A panel of Coxsackievirus B4 (CVB4) neutralizing monoclonal antibodies (mAbs) were tested against a panel of normal mouse tissues. One mAb, 356-1, reacted specifically with murine heart tissue. Immunohistochemical studies revealed an A band pattern of staining of the heart. Examination of sequential differential extracts of heart by Western immunoblotting showed that 356-1 predominantly reacted with the murine cardiac myosin heavy chain. A rather weak cross-reaction was found with actin. These observations were confirmed by the binding of 356-1 to purified cardiac myosin and actin. This antibody showed a higher affinity for murine cardiac muscle myosin than for skeletal muscle myosin. Examination of the reactivity of 356-1 with CVB4 polypeptides using Western immunoblotting revealed that 356-1 binds to the VP-1 capsid protein. These studies imply that molecular mimicry is one mechanism by which autoimmunity could develop during CVB4 induced myocarditis.
AB - A panel of Coxsackievirus B4 (CVB4) neutralizing monoclonal antibodies (mAbs) were tested against a panel of normal mouse tissues. One mAb, 356-1, reacted specifically with murine heart tissue. Immunohistochemical studies revealed an A band pattern of staining of the heart. Examination of sequential differential extracts of heart by Western immunoblotting showed that 356-1 predominantly reacted with the murine cardiac myosin heavy chain. A rather weak cross-reaction was found with actin. These observations were confirmed by the binding of 356-1 to purified cardiac myosin and actin. This antibody showed a higher affinity for murine cardiac muscle myosin than for skeletal muscle myosin. Examination of the reactivity of 356-1 with CVB4 polypeptides using Western immunoblotting revealed that 356-1 binds to the VP-1 capsid protein. These studies imply that molecular mimicry is one mechanism by which autoimmunity could develop during CVB4 induced myocarditis.
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U2 - 10.1016/0882-4010(90)90079-6
DO - 10.1016/0882-4010(90)90079-6
M3 - Article
C2 - 2161486
AN - SCOPUS:0025158339
VL - 8
SP - 151
EP - 156
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
IS - 2
ER -