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. Author manuscript; available in PMC: 2016 Apr 4.
Published in final edited form as: Curr Opin Virol. 2015 Apr 4;11:113–121. doi: 10.1016/j.coviro.2015.03.006

Table 1.

Broadly neutralizing or cross-reactive epitopes on influenza virus HA

Antibody Source IEDB1 ID HA subtype Contacts on HA12 Contacts on HA2 Crystal structure (PDB3 ID and viral HA) Reference
CR9114 human VH 1-69 178112 14/16 A subtypes and B H5: H44, Q46, D47, I48, S304, M305, P306 V364, D365, G366, W367, A382, K384, T387, Q388, I391, D392, V394, T395, V398, I402 4FQI A/Vietnam/1203/2004 [32]
CR9114 human VH1-69 178113 14/16 A subtypes and B H7: N53, T55, E56, T57, N307, L308, P309 I366, D367, G368, W369, A384, Y386, T389, Q390, I393, D394, I396, T397, L400, I404 4FQV A/Netherlands/219/2003(H7 N7) [32]
CR9114 human VH1-69 178114 14/16 A subtypes and B H3: N54, T56, E57, L58, D307, K308, P309 I363, D364, G365, W366, A381, L383, T386, Q387, I390, D391, I393, N394, L397, I401 4FQY (Hong Kong/68 H3) [32]
F16 human VH3-30*18 164106 H1, H2, H5, H6, H8, H9, H3, H4, H7, H10 H1: H45, S46, S306, T333 V362, D363, G364, W365, L382, K385, T386, Q387, N388, I389, D390, T393, N397, I400, E401 3ZTN (Calif/04/2009 H1), 3ZTJ (Aichi/68 H3) [33]
F10 human phage display 229014 H1, H2, H5, H6, H8, H9, H11 H24, H44, Q46, S304, M305 V364, D365, G366, W367, K384, T387, Q388, I391, T395, V398, N399, I402 3FKU Vietnam/1203/2004 [20]
CR6261 human VH1-69 226309 Group 1 (H1, H2, H5, H6, H8, H9) H25, H45, V46, N47, L496, S306, L307, P308, T333 D363, G364, W365, Q382, T385, Q386, I389, D390, T393, V396, N397, I400 3GBN (SouthCarolina/1918, H1), 3GBM (H5). Only H chain is bound [19,34]
S139/1 mouse 176782 H1, H2, H3, H13, and H16 receptor site H3: Y115, T148, G151, G152, S153, S154, W170, Y172, K173, S174, G175, S176, K206, E207, N210, L211, V213, L243 4GMS Victoria/3/75 [22]
C179 mouse 186645 H1, H2, H5, H6, H9 H2: H43, K45, I47, T302, L303, P304, T329 V358, D359, G360, W361, K378, T381, Q382, K383, F385, D386, V392, I396 I362, D363, G364, W365, Q382, 4HLZ Japan/305/1957 [17,18]
3.1 human VH3-30 227882 H1, H2, H5, H6 H45, V47, N48, L49, N304, S305, S306, L307, P308, T333; T385, Q386, I389, T393, V396, N397, I400; 4PY8 South Carolina/1/1918 [35]
C05 human 180352 H1, H2, H3, H9 Y114, T147, N149, G150, G151, S152, N153, S161, W169, T171, K172, Q205, E206, T208, S209, L210, L242 4FQR Aichi/1968 H3) [36]
1F2, 1F4, and 1E1 human 177664 H1 H3 H9 FIEGGWTGMVDGWYGYHH, part of fusion peptide [37]
CR8020 human 167844 H3, H7, H10 E341; E360, G361, I363, D364, R370, E375, T377, G378, Q379, A380, A381, L383, N491, E495 3SDY (Hong Kong/1/68 H3) [38]
CR8043 (similar to CR8020) human 196975 H3, H10, less H7 P37, E341, K342 E360, G361, I363, D364, R370, T377, Q379, L383 4NM8 HK/1/1968 [39]
F045-092 VH1-69 human 227712 H1, H2 H3 Y115, T148, N150, G151, G152, S153, S154, S162, W170, Y172, K173, S174, G175, N210, L211, L243 4O58 Victoria/3/75 [40] [23]
PN-SIA49 human VH3-23 0 H1, H2, H5 Group 1 Mutations that reduce binding: H25A, N336A, P338A M360A,D362A, G363A, W364A, T384A, V395A,N396A, E400A (sequence numbering refers to A/PR/8/34 [41]
39.29 human 189321 H1, H3 H34, V36, N54, S70, K292, N294, P305, D307, T334, V363, D364, G365, W366, Q379, A380, D382, L383, K384, T386, Q387, I390, D391, I393, N394, G395, L397, N398, I401, K403, T404, N405, R498 4KVN Perth/16/2009 [42]
1F1 human 179938 Various H1 K147, V149, S159, W167, K170, S173, H197, P200, T201, T203, D204, Q206, S207, L208, Q210, K236, D239, A241, G242 4GXU South Carolina/1/1918 [43]
2D1 human 164527 H1 1918 and 2009 (not seasonal H1) S138, S139, P141, N142, K171, G172, S173, S174, Y175, P176, K177, S179, K180, S181, V183, N211, E260, T262 3LZF (S.Carolina/1918 H1) 3LZG (Cal/04/2009 H1) H+L binding [27] [44]
5J8 human 191110 Seasonal and 2009 H1 except NewCal & Brisbane K147, V149, T150, A151, G157, A158, K159, W167, A203, D204, Q206, S207, L208, K236, D239, Q240 4M5Z California/07/2009 [26]
CH65 human 159269 most H1 receptor site G147, V148, S149, A150, W166, T168, G169, N171, G172, L173, N200, G202, D203, R205, A206, L207, K235, D238, R239, E240 3SM5 (Solomon Is/3/06 H1) [21]
CH67 human 180309 H1N1 1986–2007 G147, V148, S149, A150, W166, T168, N171, G172, L173, N200, G202, D203, R205, A206, L207, H209, K232, D238 4HKX Solomon Islands/3/2006 [45]
GC0587 mouse 226441 H1 T89, A90, S127, E129, R130, E132, P135, S138, K180, K186, K188, Y270, A273 4LVH Korea/1/2009 H1N1 [46]
GC0757 mouse 190190 E129, R130, F131, E132, P135, T137, S138, K180, S181, I183, Y270 4F15 Korea/1/2009 H1N1 [47]
2G1 human VH1-69 181066 H2 human and swine T138, Q139, T141, G144, G145, S146, R147, P155, T165, K166, K167, G168, S169, T203, L204 4HG4 Japan/305/1957 [24]
8F8 human VH3-33 181071 H2 human and swine T141, T143, G144, G145, S146, R147, A150, G153, N154, P155, W163, T165, E166, G168, T199, E200, T203, L204, Q236 4HF5 Japan/305/1957 [24]
8M2 human VH1-69 181067 H2 human and swine T141, T143, G144, G145, S146, R147, P155, W163, T165, K166, G168, S169, N196, D197, E198, T199, E200, R202, T203, L204, K232, G235, L236, G237, S238 4HFU Japan/305/1957 [24]
B-1, D-1 human 115630, 115652 H3 many strains Within 189–197 NFDKLYIWG and 227–239 SSRISIYWTIVKP [48]
F005-126 human 233323 H3 1968–2004 S107, K108, N187, D188, N189, P255, G256, S286, D287, A288, P289, P300, N301 3WHE Aichi/68 [49]
100F4 human 0 H5 most clades 68, 112, 137, 143, 251, 254, and 255 [50]
65C6 human 164481 H5 all clades except 7.2 118, 121, 161, 164, and 167 (mature H5 numbering) P134, S137, K177, Y180, T183 (IEDB) [51]
9F4 mouse 136074 H5 clades 271–281, centered on 272–275 [52,53]
AVFluIgG 01 human 170144 H5 I132, I133, P134, W138, S139, Y180, T183 [54]
H5M9 mouse 194677 most H5N1 clades D59, D61, V63, K64, R69, E85, N88, P90, E91, H126, E128, E286, Y287, N289, N291 4MHH Vietnam/1203/2004 [55]
HA-7 mouse 186786 H5 several clades 88–90 NVP and 126–131 HFEKIQ cryoEM [56]
CR8059 human VH1-18 178109 B strains T52, K53, S54, H55, F56, K67, N74, T76, D77, H100, E101, G300, S301, L302, P303 4FQK B/Brisbane/60/2008 [32]
CR8071 human VH1-18 178108 Most B strains T52, K53, Y55, F56, K67, L73, N74, C75, T76, D77, H100, E101, V105, G299, S300, L301, P302, I304 4FQJ B/Florida/4/2006 [32]
1

Immune Epitope Database www.iedb.org

2

Numbering is from the initiating Met and is continuous through the signal peptide and across the HA1-HA2 junction. In most crystal structures the numbering is separate for HA1 and HA2, and it often follows homology to H3 HA.