Identification of five different IGHV gene families in owl monkeys (<i>Aotus nancymaae</i>)

Hernández, E. C.; Suárez, Carlos F.; Parra, Carlos; Patarroyo, Manuel A.

doi:10.1111/j.1399-0039.2005.00491.x

Cited by 7 publications

(4 citation statements)

References 45 publications

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“…The reliance of the dual-specific antibodies that we isolated on specific human VH3-30 f alleles suggests that mice, which do not have the counterparts of human VH3-30 f genes, may not be the most suitable model organism to test a novel CSP-based vaccine. Rather, an organism such as the Aotus monkey, which has a more similar VH gene repertoire to humans and contains VH3-30 f -like genes carrying the equivalent of W52 30 , may be a more suitable choice.…”

Section: Immunization Of Mice With the Npdp19 Peptide Generates A Robmentioning

confidence: 99%

A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein

Tan

Sack

Oyen

et al. 2018

Nat Med

198

280

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Immunization with attenuated Plasmodium falciparum sporozoites (PfSPZ) has been shown to be protective, but the features of the antibody response induced by this treatment remain unclear. To investigate this response at high resolution, we isolated IgM and IgG monoclonal antibodies from Tanzanian volunteers who were immunized by repeated injection of irradiated PfSPZ and who were found to be protected from controlled human malaria infection (CHMI) with infectious homologous PfSPZ. All IgG monoclonals isolated bound to P. falciparum circumsporozoite protein (PfCSP) and recognized distinct epitopes in the N-terminus, NANP repeat region, and C-terminus. Strikingly, the most effective antibodies, as assessed in a humanized mouse model, bound not only to the repeat region, but also to a minimal peptide at the PfCSP N-terminal junction that is not in the RTS,S vaccine. These dual-specific antibodies were isolated from different donors and used VH3-30 or VH3-33 alleles carrying tryptophan or arginine at position 52. Using structural and mutational data, we describe the elements required for germline recognition and affinity maturation. Our study provides potent neutralizing antibodies and relevant information for lineage-targeted vaccine design and immunization strategies.

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Section: Immunization Of Mice With the Npdp19 Peptide Generates A Robmentioning

confidence: 99%

A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein

Tan

Sack

Oyen

et al. 2018

Nat Med

198

280

View full text Add to dashboard Cite

show abstract

“…Based on this data, for developing a logical and rational vaccine methodology at the molecular level, we decided to analyze these monkeys’ immune system molecules by cloning and sequencing the Aotus genes encoding immunoglobulins, cytokines, Class I and II molecules, and TCR α, β, δ, and δ chains, which revealed striking homology with their human counterparts. − …”

Section: Genetic Constraints Regarding Aotus Monkeys’ Immune Response...mentioning

confidence: 99%

Structural and Immunological Principles Leading to Chemically Synthesized, Multiantigenic, Multistage, Minimal Subunit-Based Vaccine Development

2011

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“…We have shown (at molecular level) that immunoglobulin [88,89], cytokines [90], major histocompatibility complex (MHC)-related genes such as class I [91], HLA-DR-related [92], HLA-DQlike [93], T-cell receptor (TCR) [94], [95], [96], [97] chains, etc. display 88%-100% homology with human nucleotide and amino acid sequences by cloning and sequencing Aotus monkeys' most relevant immune system molecules.…”

Section: Recognising and Characterising Protein Binding Sequences: Idmentioning

confidence: 99%

Functional, Immunological and Three-Dimensional Analysis of Chemically Synthesised Sporozoite Peptides as Components of a Fully-Effective Antimalarial Vaccine

Curtidor¹,

Vanegas

Alba

et al. 2011

CMC

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Our ongoing search for a fully-effective vaccine against the Plasmodium falciparum parasite (causing the most lethal form of human malaria) has been focused on identifying and characterising proteins' amino acid sequences (high activity binding peptides or HABPs) involved in parasite invasion of red blood cells (RBC) by the merozoite and hepatocytes by the sporozoite. Many such merozoite HABPs have been recognised and molecularly and structurally characterised; however, native HABPs are immunologically silent since they do not induce any immune response or protection against P. falciparum malaria infection and they have to be structurally modified to allow them to fit perfectly into immune system molecules. A deeply structural analysis of these conserved merozoite HABPs and their modified analogues has led to rules or principles becoming recognised for constructing a logical and rational methodology for a minimal subunit-based, multi-epitope, multi-stage, chemically-synthesised vaccine. The same in-depth analysis of the most relevant sporozoite proteins involved in sporozoite cell-traversal and hepatocyte invasion as well as the hepatic stage is shown here. Specifically modifying these HABPs has resulted in a new set of potential pre-erythrocyte targets which are able to induce high, longlasting antibody titres in Aotus monkeys, against their corresponding recombinant proteins and the complete parasite native molecules. This review shows how these rules may be applied against the first stage of parasite invasion (i.e. the sporozoite) to mount the first line of defence against the malarial parasite, which may indeed be the most effective one. Our results strongly support including some of these modified sporozoite HABPs in combination with the previously-described modified merozoite HABPs for obtaining the aforementioned fully-protective, multiepitope, multi-stage, minimal subunit-based, chemically-synthesized, antimalarial vaccine.

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Identification of five different IGHV gene families in owl monkeys (Aotus nancymaae)

Cited by 7 publications

References 45 publications

A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein

A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein

Structural and Immunological Principles Leading to Chemically Synthesized, Multiantigenic, Multistage, Minimal Subunit-Based Vaccine Development

Functional, Immunological and Three-Dimensional Analysis of Chemically Synthesised Sporozoite Peptides as Components of a Fully-Effective Antimalarial Vaccine

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