2017
DOI: 10.1371/journal.pone.0180999
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Spatial location of neutralizing and non-neutralizing B cell epitopes on domain 1 of ricin toxin’s binding subunit

Abstract: Ricin toxin’s binding subunit (RTB) is a galactose-/N-acetylgalactosamine (Gal/GalNac)-specific lectin that mediates uptake and intracellular trafficking of ricin within mammalian cells. Structurally, RTB consists of two globular domains, each divided into three homologous sub-domains (α, β, γ). In this report, we describe five new murine IgG monoclonal antibodies (mAbs) against RTB: MH3, 8A1, 8B3, LF1, and LC5. The mAbs have similar binding affinities (KD) for ricin holotoxin, but displayed a wide range of in… Show more

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Cited by 18 publications
(47 citation statements)
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“…We next examined the capacity of ricin‐specific MAbs to protect KCs against ricin toxicity ex vivo. We have previously described a collection anti‐RTA and anti‐RTB MAbs with a range of neutralizing activities (IC 50 ) on Vero cells . The anti‐RTA MAbs are directed against 4 spatially distinct epitope clusters (I–IV).…”
Section: Resultsmentioning
confidence: 99%
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“…We next examined the capacity of ricin‐specific MAbs to protect KCs against ricin toxicity ex vivo. We have previously described a collection anti‐RTA and anti‐RTB MAbs with a range of neutralizing activities (IC 50 ) on Vero cells . The anti‐RTA MAbs are directed against 4 spatially distinct epitope clusters (I–IV).…”
Section: Resultsmentioning
confidence: 99%
“…The results of the ex vivo studies prompted us to examine the degree to which individual anti‐ricin MAbs are able to protect KCs in vivo. We chose PB10 (anti‐RTA) and SylH3 (anti‐RTB) for these studies as they represent 2 of our most potent classes of toxin‐neutralizing MAbs . Ricin was injected into mice by the i.p.…”
Section: Resultsmentioning
confidence: 99%
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“…V5B1 was also unable to recognize R-ASF, presumably because its epitope is near the domain 1 Gal-specific binding element (5). We recently identified three additional MAbs specific for RTB's domain 1, although they were not included in this study (37).…”
Section: Fig 2 Relationships Between V H H Binding Affinities and Toxmentioning
confidence: 99%
“…Neutralizing antibodies are relatively rare, estimated at ϳ10% of the total ricin-specific pool. Complicating matters is the fact that there is often a disconnect between in vitro toxin-neutralizing activity and the capacity of a given MAb to neutralize ricin in an animal model (28,33). In other words, MAbs that have potent toxin-neutralizing activity in a cell-based assay may or may not passively protect mice from ricin intoxication.…”
mentioning
confidence: 99%