@article{fdi:010064821,
  title = {{T}he {A}nopheles-midgut {APN}1 structure reveals a new malaria transmission-blocking vaccine epitope},
  author = {{A}tkinson, {S}. {C}. and {A}rmistead, {J}. {S}. and {M}athias, {D}. {K}. and {S}andeu, {M}. {M}. and {T}ao, {D}. {Y}. and {B}orhani-{D}izaji, {N}. and {T}arimo, {B}. {B}. and {M}orlais, {I}sabelle and {D}inglasan, {R}. {R}. and {B}org, {N}. {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{M}osquito-based malaria transmission-blocking vaccines (m{TBV}s) target midgut-surface antigens of the {P}lasmodium parasite's obligate vector, the {A}nopheles mosquito. {T}he alanyl aminopeptidase {N} ({A}n{APN}1) is the leading m{TBV} immunogen; however, {A}n{APN}1's role in {P}lasmodium infection of the mosquito and how anti-{A}n{APN}1 antibodies functionally block parasite transmission have remained elusive. {H}ere we present the 2.65-angstrom crystal structure of {A}n{APN}1 and the immunoreactivity and transmission-blocking profiles of three monoclonal antibodies (m{A}bs) to {A}n{APN}1, including m{A}b 4{H}5{B}7, which effectively blocks transmission of natural strains of {P}lasmodium falciparum. {U}sing the {A}n{APN}1 structure, we map the conformation-dependent 4{H}5{B}7 neoepitope to a previously uncharacterized region on domain 1 and further demonstrate that nonhuman-primate neoepitope-specific {I}g{G} also blocks parasite transmission. {W}e discuss the prospect of a new biological function of {A}n{APN}1 as a receptor for {P}lasmodium in the mosquito midgut and the implications for redesigning the {A}n{APN}1 m{TBV}.},
  keywords = {},
  booktitle = {},
  journal = {{N}ature {S}tructural and {M}olecular {B}iology},
  volume = {22},
  numero = {7},
  pages = {532--539},
  ISSN = {1545-9993},
  year = {2015},
  DOI = {10.1038/nsmb.3048},
  URL = {https://www.documentation.ird.fr/hor/fdi:010064821},
}