The effect of molybdenum-induced copper deficiency on acute-phase protein concentrations, superoxide dismutase activity, leukocyte numbers, and lymphocyte proliferation in beef heifers inoculated with bovine herpesvirus-1.
This study was conducted to determine the effect of Cu deficiency on acute-phase protein concentrations, superoxide dismutase activity, leukocyte numbers, and lymphocyte proliferation in heifers inoculated with live bovine herpesvirus-1 (BHV-1). Hereford x Angus heifers were allotted by weight and initial liver Cu concentrations into molybdenum (Mo)-supplemented (n = 6) or control (n = 6) groups. Control heifers were fed a basal diet supplemented with Cu-sulfate to achieve a dietary concentration of 8 ppm of Cu. The Mo-supplemented heifers received the basal diet supplemented with Mo to achieve a dietary Mo:Cu ratio of 2.5:1 and with sulfur at .3% of the diet. All treatments were delivered for 129 d, when heifers were inoculated intranasally with BHV-1. To ensure adequate Cu stores before viral challenge, control heifers were given a cupric glycinate injection on d 100 of treatment. On d 129, Mo-supplemented heifers were considered Cu-deficient (liver Cu = 23.2 and 90.1 ppm for Mo-supplemented and control, respectively). Neutrophils were increased (P < .01) on d 129 in Mo-supplemented heifers. Ceruloplasmin, a copper-dependent acute-phase protein, increased (P < .01) by 48 h after challenge in control but not in Mo-supplemented heifers. Fibrinogen, an acute-phase protein not containing copper, increased by 48 h after challenge in Mo-supplemented but not in control heifers. Erythrocyte superoxide dismutase (SOD) activity was less (P < .05) in Mo-supplemented heifers on d 129. Viral challenge had no effect on SOD activity. Lymphocyte proliferative response to phytohemagglutinin stimulation was greater (P < .01) for Mo-supplemented heifers following BHV-1 challenge. No differences were detected when lymphocytes were stimulated with concanavalin-A or pokeweed mitogens. These data indicate that Cu deficiency alters the acute-phase protein response to viral infection and may affect lymphocyte responsiveness to mitogen stimulation.
Arthington
J D
JD
Departments of Animal Sciences and Industry, Kansas State University, Manhattan 66506-0201, USA.
Corah
L R
LR
Blecha
F
F
D000209:Acute-Phase Proteins / Q000032:analysis; D000818:Animals; D001835:Body Weight / Q000502:physiology; D002417:Cattle; D002418:Cattle Diseases / Q000276:immunology*; D002570:Ceruloplasmin / Q000032:analysis; D003300:Copper / Q000032:analysis / Q000172:deficiency* / Q000502:physiology; D004912:Erythrocytes / Q000201:enzymology; D005260:Female; D005340:Fibrinogen / Q000032:analysis; D005527:Food, Fortified; D006566:Herpesviridae Infections / Q000276:immunology / Q000662:veterinary*; D007242:Herpesvirus 1, Bovine / Q000276:immunology*; D007958:Leukocyte Count / Q000662:veterinary; D008099:Liver / Q000737:chemistry / Q000502:physiology; D008213:Lymphocyte Activation; D008982:Molybdenum / Q000008:administration & dosage / Q000009:adverse effects*; D010835:Phytohemagglutinins / Q000494:pharmacology; D011897:Random Allocation; D013482:Superoxide Dismutase / Q000032:analysis / Q000097:blood
D000209:Acute-Phase Proteins; D010835:Phytohemagglutinins; D003300:Copper; D008982:Molybdenum; D005340:Fibrinogen; D013482:Superoxide Dismutase; D002570:Ceruloplasmin