Ask about this productRelated genes to: NANP Blocking Peptide
- Gene:
- NANP NIH gene
- Name:
- N-acetylneuraminic acid phosphatase
- Previous symbol:
- C20orf147, HDHD4
- Synonyms:
- dJ694B14.3, MGC26833
- Chromosome:
- 20p11.21
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-17
- Date modifiied:
- 2016-10-05
Related products to: NANP Blocking Peptide
Related articles to: NANP Blocking Peptide
- Monoclonal antibodies (mAbs) targeting the Plasmodium falciparum circumsporozoite protein (PfCSP) have demonstrated substantial promise in preventing malaria infection and disease. PfCSP is characterized by a central region composed of repetitive NANP motifs, which serve as major targets for protective antibodies. Several potent mAbs targeting this region exhibit homotypic Fab-Fab interactions, which enhance antigen binding and contribute to their neutralization potency. Among these, mAb 399, encoded by the IGHV3-49/IGKV2D-29 (VH3-49/VK2D-29) germline lineages, forms head-to-head inter-Fab contacts mediated primarily by germline-encoded residues. Here, we determined X-ray and cryo-EM structures of two additional Fabs, derived from the same germline lineages, 7160 and 7118, in their unliganded forms and with PfCSP-derived peptides or recombinant shortened CSP. Both Fabs bound NANP6 repeats with high affinity (KD 6-10 nM). Fab 7160 formed germline-encoded inter-Fab homotypic interactions resembling Fab 399, indicating a conserved and preconfigured mode of antigen recognition. In contrast, Fab 7118 does not form homotypic contacts and adopts a distinct binding mode, which precludes inter-Fab interactions. These findings highlight the structural versatility of VH3-49/VK2D-29-derived antibodies and demonstrate that their CDR loop variations can modulate antibody conformation, homotypic Fab-Fab interactions, and epitope engagement. Our study further defines this class of germline-encoded anti-CSP antibodies and provides mechanistic insights into how they achieve high-avidity binding and protective immunity either through or independent of pre-configured Fab-Fab interactions with important implications for germline-targeting malaria vaccine design. - Source: PubMed
Publication date: 2026/06/03
Jain MonikaCannac FabienAgrawal SashankLee Wen-HsinLoeffler Johannes RFernández-Quintero Monica LGonzález-Páez Gonzalo EMoskovitz Re'emWard Andrew BWilson Ian A - The decline in protective antibody titers and efficacy over time of the circumsporozoite protein (CSP)-based RTS,S/AS01 and R21/Matrix-M vaccines highlights the need for improved vaccines. Sporozoite microneme protein essential for cell traversal-1 (SPECT-1) is a conserved () antigen that plays a key role in parasite movements while traversing host cells. Targeting SPECT-1 as an addition to the CSP in the same vaccine may enhance immune response and protection. - Source: PubMed
Publication date: 2026/05/14
Turan GulbuseMukhopadhyay EktaTruby AdamFedorova KseniiaPeralta Alvarez Marco PoloAlharbi Naif KhalafHill Adrian V SSalman Ahmed M - The RTS,S/AS01 malaria vaccine was recently approved for implementation in children, but only provides modest and short-lived efficacy against malaria. RTS,S targets a portion of the Plasmodium falciparum (Pf) circumsporozoite protein (CSP), comprising the central NANP-repeat region and C-terminal domain. Mechanisms of immunity and correlates of protection for the RTS,S vaccine are not well defined, hindering progress towards generating highly effective CSP-based vaccines. - Source: PubMed
Publication date: 2026/05/14
Hysa AlessiaOpi D HerbertWaterhouse JoshuaChishimba SandraHorton Jessica LKingston NatalieNetter Hans JWetzel DavidPiontek MichaelFeng GaoqianSacarlal JahitDobaño CarlotaKurtovic LiriyeBeeson James G - The RTS,S/AS01 malaria vaccine provides partial protection against Plasmodium falciparum, largely mediated by antibodies targeting the circumsporozoite protein. Correlates of protection remain incompletely defined and have focused mainly on peak IgG responses to the immunodominant NANP-repeats, with less known about antibody durability or responses to the C-terminus of circumsporozoite protein. - Source: PubMed
Publication date: 2026/04/21
Lara-Escandell MariaSánchez LinaMacià DídacJairoce ChenjeraiMpina MaxmillianSorgho HermannAgnandji Selidji TodagbeDosoo DavidGyan BenVidal MartaJiménez AlfonsMitchell Robert AndrewMedina-Expósito DanielPuyol LauraSantano RebecaDutta SheetijOwusu-Agyei SethAsante Kwaku PokuTinto HalidouAide PedroNhabomba AugustoMordmüeller BenjaminDaubenberger ClaudiaAguilar RuthWaitumbi JohnMoncunill GemmaDobaño Carlota - Microbial chain elongation for medium-chain fatty acid production has gained significant attention. This study elucidated how initial pH and carbon sources regulate microbial caproic acid production from organic waste. By successively subculturing pit mud with Huangshui, lactic acid, or ethanol at different pH values (4.0-6.0), we obtained two enriched consortia: NatCom H (from Huangshui) and NatCom E (from ethanol), both of which produce 10 g/L caproic acid at pH 6.0. Key functional divergence was observed: NatCom H maintained production from pH 5.0 to 6.0, whereas NatCom E was functional only at pH 6.0. Integrated multiomics and bioreactor analyses revealed that this divergence stemmed from distinct microbial interactions. NatCom H was structured around a pH-mediated mutualism between Clostridium tyrobutyricum and acid-sensitive Caproiciproducens species, engaging in sequential substrate conversion. In contrast, NatCom E was dominated solely by Clostridium kluyveri. The hypothesized interaction mechanism was confirmed by isolating the key strains (including two novel Caproiciproducens species) and constructing a synthetic community, which demonstrated that C. tyrobutyricum alleviates acidic stress for Caproiciproducens, enabling caproate synthesis at pH 5.0. These findings reveal a substrate-driven ecological strategy for environmental adaptation and provide a mechanistic framework for engineering robust consortia to convert wastes such as Huangshui into valuable caproic acid. - Source: PubMed
Publication date: 2026/04/11
Jin XiangyiFan ZhanyangYang ManqingShen HongyeLi JinshanHu YongmeiPeng NanZhao Shumiao