Influenza　A　virus　are　a　persistent　and　significant　threat　to　human　health,　and　current　vaccines　do　not　provide　sufficient　protection　due　to　antigenic　drift,　which　allows　influenza　viruses　to　easily　escape　immune　surveillance　and　antiviral　drug　activity.　Influenza　hemagglutinin　(HA)　is　a　glycoprotein　needed　for　the　entry　of　enveloped　influenza　viruses　into　host　cells　and　is　a　potential　target　for　anti-influenza　humoral　immune　responses.　In　recent　years,　a　number　of　broadly　neutralizing　antibodies　(bnAbs)　have　been　isolated,　and　their　relative　structural　information　obtained　from　the　crystallization　of　influenza　antigens　in　complex　with　bnAbs　has　provided　some　new　insights　into　future　influenza　vaccine　research.　Here,　we　review　the　current　knowledge　of　the　HA-targeted　bnAbs　and　the　structure-based　mechanisms　contributing　to　neutralization.　We　also　discuss　the　potential　for　this　structure-based　approach　to　overcome　the　challenge　of　obtaining　a　highly　desired　＂universal＂　influenza　vaccine,　especially　on　small　proteins　and　peptides.　(C)　2019　Published　by　Elsevier　B.V.　on　behalf　of　Research　Network　of　Computational　and　Structural　Biotedinology.