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Assessing Vaccine Efficacy in Different Animal Models

Testing efficacy of any new vaccine requires a disease model and gold standard controls to act as quantitative markers. The slow progression of MAP pathogenesis, the lack of reliable cor­relates of protection and the inability of current vaccines to effectively stop transmission make delivering these a logistical challenge.

Ruminant models are certainly required for the final testing of vaccines but are very expensive. As discussed above, cheaper mouse models have been used for initial screening but have shown poor pre­dictability for protection in larger animals. The problem of how to screen new LAV candidates quickly and effectively has been compounded

Table 23.4. Summary of live vector subunit and other vaccine candidates tested in animals.

Vaccine target and delivery

type

Other name(s) Size

(kDa)

Function Tested species Challenge strain Dose and route of infection Comments
Bull eta/., 2007, 2014
Fusion construct of non- AphC MAP- 95 Alkyl hydroperoxidase C57BI√6 mice Low-passage isolate 1?10,j CFU ip. Immunized sc. with Ad5 prime.
transmembrane regions from RS08085 of MAP (K37) from 2 weeks after Boost after 2 weeks.
One-
four MAP genes MAP1589c, gsd MAP_

RS06265

GPL fucosyl transferase cow with JD (prophylactic) or log decrease in spleen and
MAPI234, MAP2444c, 3 weeks before liver in both therapeutic and
MAPI235 inserted as an (therapeutic) prophylactic administration 6
expression construct into vaccination weeks (prophylactic) and 12 weeks
modified Adenovirus 5 and (therapeutic) post-challenge
Vaccinia Ankara delivery vectors p12 MAP Antisense protein to 3-week-old Low-passage isolate 1 ? 10’ CFU total Immunized id. with adenoviral
RS12460 IS900 transferase calves of MAP (R0808) from orally in two doses prime (11 weeks prior to challenge)
mρa MAP_

RS22605

GPL acetyl transferase cow with JD 5 weeks after MVA boost vaccination and vaccinia boost (5 weeks prior to challenge).
Significant two log decrease in gut mucosal load. No faecal shedding in vaccinated group at 36 weeks post-challenge
Chandra et al., 2012
Fusion constructs of partial Ag85A (202-347) 34.5 Secretable fragments 180 C57BL∕6 MAP strain 66115- 1 ? 10’ CFU Immunized ip. with 5 ? 108 CFU
proteins from MAP0216,

MAPI609c, MAP3527,

Ag85B (173-330) 33.3 of mycolyl- transferases involved mice 98 in PBS ip. 6 weeks after last in PBS or 10 μg of each purified antigen in MPLadjuvant. Boosted
MAPI519 and MAP0187c in cell wall synthesis immunization at 3 weeks. Both purified Ag and
expressing in attenuated

Salmonella species. Also purified fusion partial protein

MAP74F (1-148 &

669-786)

40.7 Secretable serine protease & PPE gene fragments Salmonella delivery induced three- log reduction in spleen and liver CFU at 16 weeks post-challenge.
mix Some decrease in histopathological
SOD (1-72) 19.5 Secretable fragments of superoxide dismutase and granuloma scores
Faisal et al., 2013b
MAP0216 Ag85A 32 Secretable fragments Goats MAP strain 66115- Seven doses Immunized sc.
5 ? 108 CFU/
of mycolyl- 98 5 ? 108 oral 3 animal. Boosted at 3 weeks
transferases involved weeks after last
in cell wall synthesis immunization
MAPI 609c Ag85B 30

Table 23.4. Continued

Vaccine target and delivery

type

Other name(s) Size

(kDa)

Function Tested species Challenge strain Dose and route of infection Comments
MAP0187c SOD 23 superoxide dismutase

Jolly et al., 2013

Lipoarabinomannan (LAM) produced by phenol/ methanol extraction of MAP culture LAM 20 Glycolipid 106-month- old Aberdeen Angus calves Local MAP strain from JD cow 1 ? 109 CFUoraI

10 days after last immunization

Immunized and boosted at 6, 12 and 24 weeks with 2 mg of LAM extract dissolved in 1 ml of PBS and emulsified in 1 ml of Freund’s Incomplete Adjuvant.
No faecal shedding in two out of two cattle in vaccine group

CFU1 colony-forming units; MAP, Mycobacterium avium subsp. paratuberculosis; sc., subcutaneous; ip., intraperitoneal; id., intradermal; PBS, phosphate buffered saline; MPL, monophosphoryl lipid A; JD, Johne’s disease.

398 T. Bull

by the apparent failure of in vitro macrophage assays.

Protective efficacy of a prophylaxic vac­cine is generally demonstrated by comparing challenge loads present in naive vs vaccinated animals after a designated immune clearance period. It is unlikely that any vaccine directed against pathogenic mycobacteria however will have sterilizing capacity; thus, comparisons against current ‘gold standard' vaccine effi­cacy are also essential. Replication in liver and spleen is usually monitored by CFU plating and when testing LAV commonly includes a selec­tion marker to monitor immunogen persistence. Examples include kanamycin or hygromycin but could also include luminometry using con­structs expressing luciferase or GFP (Rosseels et al., 2006b; Park et al., 2011). Standardized protocols for certain animal models have been proposed (Hines et al., 2007a) but not vali­dated as authoritative. If new vaccines are to be brought to the market place, a significant improvement in the manner in which trials are performed is required. New tests are needed to detect the direct presence of MAP and the host's specific responses to challenge by live MAP and many of its individual components; models re­quire rigorous standardizing and a realistic achievable output measure of efficacy related to faecal shedding is needed.

23.5

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Source: Behr Marcel A., Stevenson K., Kapur V. (eds.). Paratuberculosis: Organism, Disease, Control. 2nd edition. — CAB International,2020. — 439 p.. 2020
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