TABLE 3.

Mapping of anti-MPER neutralizing antibodies

ChimeraMPER sequenceaNeutralizationbPlasma ID50
2F54E10Z13e1BB34CAP206SAC21
7312ANMYEL660QKLNSWDVFG670NWFDLASWVK680YIQYGVYIV<2021<20
C1NMYEL660LALDKWASLW670NWFDITKWLW680YIKYGVYIV++++++5,5603,9033,871
C1CNMYEL660LALDSWKNLW670NWFDITKWLW680YIKYGVYIV++++3,9452,8672,733
C1C F/LNMYEL660LALDSWKNLW670NWLDITKWLW680YIKYGVYIV+1,7792,4491,802
C3NMYEL660LALDKWASLW670NWFDLASWVK680YIQYGVYIV++<20<20<20
C7(2F5)NMYEL660QALDKWAVFG670NWFDLASWVK680YIQYGVYIV++<20<20<20
C6(4E10)NMYEL660QKLNSWDVFG670NWFDITSWIK680YIQYGVYIV++<20<20<20
C4NMYEL660QKLNSWDVFG670NWFDITKWLW680YIKYGVYIV+++/−<20723189
C4GWNMYEL660QKLNSWDVFW670NWFDITKWLW680YIKYGVYIV++++7,4823,0672,987
C8NMYEL660QKLNSWDSLW670NWFDITKWLW680YIKYGVYIV+++3,3512,5381,199
  • a Grafted amino acids are indicated in italics, with the 7312A residues in lightface. Further mutations on the chimeras are in boldface.

  • b Neutralization by MAbs 2F5, 4E10, and Z13e1 are qualitatively indicated relative to the titers obtained with the C1 chimera. −, no neutralization; ++, neutralization similar to that of C1; +, neutralization within 3-fold of that of C1; +/−, neutralization within 10-fold of that of C1.