[en] Herpesviruses consistently transmit from immunocompetent carriers, implying that their neutralization is hard to achieve. Murid Herpesvirus-4 (MuHV-4) exploits host IgG Fc receptors to bypass blocks to cell binding, and pH-dependent protein conformation changes to unveil its fusion machinery only after endocytosis. Nevertheless neutralization remains possible by targeting the virion glycoprotein H (gH) / gL heterodimer, and the neutralizing antibody responses of MuHV-4 carriers are improved by boosting with recombinant gH/gL. We analysed here how gH/gL-directed neutralization works. The MuHV-4 gH/gL binds to heparan sulfate. However most gH/gL-specific neutralizing antibodies did not block this interaction. Nor did they act directly on fusion. Instead they blocked virion endocytosis and transport to the late endosomes where membrane fusion normally occurs. The poor endocytosis of gH/gL-neutralized virions was recapitulated precisely by virions genetically lacking gL. Therefore driving virion uptake appears to be an important function of gH/gL that provides a major target for antibody-mediated neutralization.