PMID- 6971249
OWN - NLM
STAT- MEDLINE
DCOM- 19810613
LR  - 20111117
IS  - 0171-2985 (Print)
IS  - 0171-2985 (Linking)
VI  - 158
IP  - 3
DP  - 1981
TI  - Roles of influenza virus infectivity and glycosylation of viral antigen for 
      recognition of target cells by cytolytic T lymphocytes.
PG  - 239-53
AB  - The influenza virus strains A/JAP (H2N2) and the recombinant strain A/JAP/BEL 
      (H2N1) were tested before and after UV-light inactivation for their ability to 
      sensitize target cells for cytotoxic T-cell lysis (CTL). Infectious preparations 
      were efficient sensitizers for both specific and cross-reactive CTL, exposure of 
      the cells to even low doses of virus resulting in almost maximum susceptibility. 
      When inactivated, however, A/JAP/BEL was about 10 times more efficient than A/JAP 
      at sensitizing the cells for specific CTL; neither sensitized the cells for 
      cross-reactive CTL. Thus factors other than or in addition to a cleaved 
      haemagglutinin (HA) molecule are important in the fusion of the virus with the 
      cell membrane. Target cells which were infected with virus and exposed to 
      different concentrations of tunicamycin, which inhibits glycosylation, became 
      susceptible to CTL by both specific and cross-reactive effector cells through to 
      a lesser extent than controls. Infected cells showed both strong haemadsorption 
      and cocapping of the HA with K, D gene products. Both of these properties were 
      greatly diminished in the presence of even low concentrations of tunicamycin. 
      Analysis of binding studies using labelled monoclonal anti-HA IgG showed that, in 
      the presence of tunicamycin, the total amount of HA expressed at the cell surface 
      was not reduced, but there was an increase in the dissociation constant of the 
      reaction between expressed HA and antibody. This latter finding was thought to 
      reflect a conformational change in the HA antigen, which might be the reason for 
      the reduced susceptibility to CTL.
FAU - Ertl, H
AU  - Ertl H
FAU - Ada, G L
AU  - Ada GL
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Immunobiology
JT  - Immunobiology
JID - 8002742
RN  - 0 (Antigens, Viral)
RN  - 0 (H-2 Antigens)
RN  - 0 (Hemagglutinins)
RN  - 11089-65-9 (Tunicamycin)
SB  - IM
MH  - Animals
MH  - Antigens, Viral/*immunology
MH  - Binding Sites, Antibody
MH  - *Carbohydrate Metabolism
MH  - *Cytotoxicity, Immunologic
MH  - Female
MH  - H-2 Antigens/immunology
MH  - Hemagglutinins/immunology
MH  - Immunity, Cellular
MH  - Immunologic Capping/drug effects
MH  - Influenza A virus/immunology
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Orthomyxoviridae Infections/*immunology
MH  - Sheep
MH  - T-Lymphocytes/immunology
MH  - Tunicamycin/pharmacology
EDAT- 1981/01/01 00:00
MHDA- 1981/01/01 00:01
CRDT- 1981/01/01 00:00
PHST- 1981/01/01 00:00 [pubmed]
PHST- 1981/01/01 00:01 [medline]
PHST- 1981/01/01 00:00 [entrez]
AID - S0171-2985(81)80073-3 [pii]
AID - 10.1016/S0171-2985(81)80073-3 [doi]
PST - ppublish
SO  - Immunobiology. 1981;158(3):239-53. doi: 10.1016/S0171-2985(81)80073-3.